Abstract
Proteins can be conveniently divided into two groups on the basis of their composition: simple proteins, which only contain amino acids and conjugated proteins which have in addition nonamino acid components as prosthetic groups. In plants, a wide range of conjugated proteins are present, which contain covalently linked carbohydrates either as glycoproteins, in which the protein component is substituted by one or more heterosaccharides with a relatively low number (2–15) of sugar residues, or as proteoglycans, in which the protein component carries polysaccharide substituents (Marshall and Neuberger 1970, Gottschalk 1972a, Kornfeld and Kornfeld 1976, Clarke et al. 1979). As more examples are being discovered, it appears that these two classes represent the ends of a continuous range of macromolecules containing both protein and carbohydrate. The main emphasis of this chapter will be on the biochemistry of intracellular glycoproteins of higher plants. Some comparisons with intra- and extra-cellular proteoglycans and cell wall glycoproteins of higher plants and glycoproteins of animals and micro-organisms will be made to highlight certain common structural features, associations, localization, and functions. Such a comparative study, besides indicating the significance of these macromolecules in living organisms, may also stimulate areas for future research.
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References
Agrawal BBL, Goldstein IJ (1967) Physical and chemical characterization of Concanavalin A, the hemagglutinin from Jack Bean (Canavalia ensiformis). Biochim Biophys Acta 133: 376–379
Akiyama Y, Kato K (1976) Hydroxyproline arabinosides from suspension-cultured tobacco cell wall. Agric Biol Chem 40: 2343–2348
Akiyama Y, Kato K (1977) Structure of hydroxyproline-arabinosides from tobacco cells. Agric Biol Chem 41: 79–81
Akiyama Y, Mori M, Kato K (1980) 13C-NMR analysis of hydroxyproline arabinosides from Nicotiana tabacum Agric Biol Chem (Tokyo) 44: 2487–2489
Allen AK, Neuberger A (1973) The purification and properties of the lectin from potato tubers, a hydroxyproline containing glycoprotein. Biochem J 135: 307–314
Allen AK, Neuberger A (1975) A simple method for the preparation of an affinity adsorbent for soybean agglutinin using galactosamine and CH-Sepharose. FEBS lett 50: 362–364
Allen AK, Neuberger A, Sharon N (1973) The purification, composition and specificity of wheat-germ agglutinin. Biochem J 131: 155–162
Allen AK, Desai NN, Neuberger A (1976) The purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity. Biochem J 155: 127–135
Allen AK, Desai NN, Neuberger A, Creeth JM (1978) Properties of potato lectin and the nature of its glycoprotein linkages. Biochem J 171: 665–674
Anderson RL, Clarke AE, Jermyn MA, Knox RB, Stone BA (1977) A carbohydrate-binding arabinogalactan-protein from liquid suspension cultured endosperm from Lolium multi- florum. Aust J Plant Physiol 4: 143–158
Anderson S, Wold JK (1978) Water soluble glycoproteins from Urtica dioica. Phytochemistry 17: 1875–1877
Andrews AT (1974) Navy (Haricot)-bean (Phaseolus vulgaris) lectin. Isolation and characterization of two components from a toxic agglutinating extract. Biochem J 139: 421–429
Andrews P (1965) The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J 96: 595–606
Andrews P (1970) Estimation of molecular weight size and molecular weights of biological compounds by gel-filtration. In: Glick D (ed) Methods of biochemical analysis, vol XVIII. Interscience Publ New York, pp 1–53
Arnold WN (1966) β-fructofuranosidase from grape berries. 111. The identity of the soluble and bound fractions. Biochim Biophys Acta 128:196–198
Auber J-P, Biserte G, Loucheux-Lefebvre MH (1976) Carbohydrate-peptide linkage in glycoproteins. Arch Biochem Biophys 175: 410–418
Baenziger J, Kornfeld S (1974a) Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation and structures of the asparagine-linked oligosaccharide units. J Biol Chem 249: 7260-7269
Baenziger J, Kornfeld S (1974b) Structure of the carbohydrate unit of IgA1 immunoglobulin. 11. Structure of the O-glycosidically linked oligosaccharide unit. J Biol Chem 249: 7270–7281
Bailey CJ, Boulter D (1970) The structure of legumin, a storage protein of broad bean (Vicia faba) seeds. Eur J Biochem 17: 460–466
Bain JM, Mercer FV (1966) Subcellular organization of the developing cotyledons of Pisum sativum L. Aust J Biol Sci 19: 49–67
Barnett J A (1976) The utilization of sugars by yeast. In: Tipson RS, Horton D (eds) Advances in carbohydrate chemistry and biochemistry, vol XXXII. Academic Press, London New York, pp 125–234
Basha SM, Beevers L (1975) The development of proteolytic activity and protein degradation during germination of Pisum sativum L. Planta 124: 77–87
Basha SM, Beevers L (1976) Glycoprotein metabolism in the cotyledons of Pisum sativum during development and germination. Plant Physiol 57: 93–97
Baumann C, Rudiger H, Strosberg AD (1979) A comparison of the two lectins from Vicia cracca. FEBS lett 102: 216–218
Beevers L, Guernsey FS (1966) Changes in some nitrogenous components during the germination of pea seeds. Plant Physiol 41: 1455–1458
Beevers L, Splittstoesser WE (1968) Protein and nucleic acid metabolism in germinating peas. J Exp Bot 19: 698–711
Beytia ED, Porter JW (1976) Biochemistry of polyisoprenoid biosynthesis. Annu Rev Biochem 45: 113–142
Bhatia HM, Khim YG, Boyd WC (1968) Serological and immunochemical characterization of the lima bean anti-A lectin. Vox Sang 15: 278–286
Blagrove RJ, Gillespie JM (1975) Isolation, purification and characterization of the seed globulin of Lupinus angustifolius. Aust J Plant Physiol 2: 13–27
Bogdanov V, Kaverzneva E, Andrejeva A (1962) New data on the link between the polysaccharide prosthetic group and protein in ovalbumin. Biochim Biophys Acta 65: 168–169
Boundy JA, Wall JS, Turner JE, Woychik JH, Dimler RJ (1967) A mucopolysaccharide containing hydroxyproline from corn pericarp. Isolation and composition. J Biol Chem 242: 2410–2415
Boyd WC, Reguera RMJ (1949) Hemagglutinin substances for human cells in various plants. J Immunol 62: 333–339
Boyd WC, Shapleigh E, McMaster M (1955) Immunochemical behaviour of a plant agglutinin (lectin). Arch Biochem Biophys 55: 226–234
Bray BA, Lieberman R, Meyer K (1967) Structure of human kerato-sulphate. The linkage region. J Biol Chem 242: 3373–3380
Browder SK, Beevers L (1978) Characterization of the glycopeptide bond in legumin from Pisum sativum L. FEBS lett 89: 145–148
Brown JA, Segal HL, Maley F, Trimble RB, Chu FK (1979) Effect of deglycosylation of yeast invertase on its uptake and digestion in rat yolk sacs. J Biol Chem 254: 3689–3691
Brown RG, Kimmins WC (1977) Glycoproteins. In: Northcote DH (ed) International reviews of biochemistry, vol XIII. (Plant Biochem 11). Univ Park Press, Baltimore, pp 183–209
Brown RG, Kimmins WC (1978) Protein polysaccharide linkages in glycoproteins from Phaseolus vulgaris. Phytochemistry 17: 29–33
Brown RG, Kimmins WC, Lindberg B (1974) Structural studies of glycoproteins from Phaseolus vulgaris. Acta Chem Scand B29: 4–13
Brysk M,. Chrispeels MJ (1972) Isolation and partial characterization of a hydroxyproline- rich cell wall glycoprotein and its cytoplasmic precursors. Biochim Biophys Acta 257: 421–432
Bunn HF, Gabbay KH, Gallop PM (1978) The glycosylation of hemaglobin: relevance to diabetes mellitus. Science 200: 21–27
Casey R (1979) Immunoaffinity chromatography as a means of purifying legumin from Pisum (pea) seeds. Biochem J 177: 509–520
Castimpoolas N (1969) A note on the proposal of an immunochemical system of reference and nomenclature for the major soybean globulins. Cereal Chem 46: 369–372
Castimpoolas N, Ekenstam C (1969) Isolation of alpha, beta and gamma conglycinins. Arch Biochem Biophys 129: 490–497
Castimpoolas N, Meyer EW (1969) Isolation of soybean hemagglutinin and demonstration of multiple forms by isoelectric focusing. Arch Biochem Biophys 132: 279–285
Castimpoolas N, Leuther E, Meyer EW (1968) Studies on the characterization of soybean proteins by immunoelectrophoresis. Arch Biochem Biophys 127: 338–345
Catt JW, Hills GJ, Roberts K (1976) A structural glycoprotein containing hydroxyproline isolated from the cell wall of Chlamydomonas reinhardii. Planta 131: 165–171
Catt JW, Hills GJ, Roberts K (1978) Cell wall glycoproteins from Chlamydomonas reinhardii, and their self-assembly. Planta 138: 91–98
Cawley DB, Hedblom ML, Houston LL (1978) Homology between ricin and Ricinus communis agglutinin: Amino acid terminal sequence analysis and protein synthesis inhibition studies. Arch Biochem Biophys 190: 744–755
Cho Y-P, Chrispeels MJ (1976) Serine-O-galactosyl linkages in glycopeptides from carrot cell walls. Phytochemistry 15: 165–169
Chu FK, Trimble RB, Maley F (1978) The effect of carbohydrate depletion on the properties of yeast external invertase. J Biol Chem 253: 8691–8693
Clark JF, Jakoby WB (1970) Yeast aldehyde dehydrogenase. 111. Preparation of three homogeneous species. J Biol Chem 245: 6065–6071
Clarke AE, Knox RB (1978) Cell recognition in flowering plants. Q Rev Biol 53: 3–28
Clarke AE, Knox RB, Jermyn MA (1975) Localization of lectins in legume cotyledons. J Cell Sci 19: 157–161
Clarke AE, Anderson RL, Stone BA (1979) Form and function of arabinogalactans and arabinogalactan-proteins. Phytochemistry 18: 521–540
Clarke J, Shannon LM (1976) The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzyme C. Biochim Biophys Acta 427: 428–433
Cleland R, Karlsnes AM (1967) A possible role of hydroxyproline-containing proteins in the cessation of cell elongation. Plant Physiol 42: 669–671
Croy RRD (1977) The localization of the major proteins and proteolytic enzymes in Phaseolus vulgaris L., at germination. PhD Thesis, Univ Aberdeen, UK
Cunningham BA, Wang JL, Waxdal MJ, Edelman GM (1975) The covalent and three- dimensional structure of Concanavalin A. 11. Amino acid sequence of cyanogen bromide fragment F3. J Biol Chem 250: 1503–1512
Dahlgren K, Porath J, Lindahl-Kiessling K (1970) On the purification of phytohemagglutinins from Phaseolus vulgaris. Arch Biochem Biophys 137: 306–314
Danielsson CE (1949) Seed globulins of the Gramineae and Leguminosae. Biochem J 44: 387–400
Danielsson CE, Lis H (1952) Differences in the composition of some pea proteins. Acta Chem Scand 6: 139–148
Davey RA, Dudman WF (1979) The carbohydrate of storage glycoproteins from seeds of Pisum sativum: Characterization and distribution of component polypeptides. Aust J Plant Physiol 6: 435–447
Delmotte F, Kieda C, Monsigny M (1975) Protein-sugar interaction by affinity chromatography of Solanum tuberosum agglutinin ( STA-lectin ). FEBS lett 53: 324–330
Derbyshire E, Wright DJ, Boulter D (1976) Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 15: 2–24
Desai NN, Allen AK (1979) The purification of potato lectin by affinity chromatography on an N, N′, N″-triacetylchitotriose-Sepharose matrix. Anal Biochem 93: 88–90
Deyl Z (1976) Advances in separation techniques in sequence analysis of proteins and peptides. J Chromatogr 127: 91–132
Diezel W, Bohme HJ, Nissler K, Freyer R, Heilman W, Kopperschlager G, Hofman E (1973) A new purification procedure for yeast phosphofructokinase minimizing proteolytic degradation. Eur J Biochem 38: 479–488
Dougall DK, Shimbayashi K (1960) Factors affecting growth of tobacco callus tissue and its incorporation of tyrosine. Plant Physiol 35: 294–303
Driessche Van E, Foriers A, Strosberg AD, Kanarek L (1976) N-terminal sequences of the α- and β-subunits of the lectin from the garden pea (Pisum sativum). FEBS Lett 71: 220–222
Dunn MJ, Maddy AH (1976) Techniques for the analysis of membrane proteins. In: Maddy AH (ed) Biochemical analysis of membranes. Chapman and Hall, London, pp 197–251
Dutton GGS (1973) Applications of gas-liquid chromatography to carbohydrates: Part 1. In: Tipson RS, Horton D (eds) Advances in carbohydrate chemistry and biochemistry, vol XXVIII. Academic Press, London New York, pp 11–160
Eastcoe JE (1972) Amino acid analysis of glycoproteins. In: Gottschalk A (ed) Glycoproteins: Their composition, structure and function, 2nd edn, part A. Elsevier, Amsterdam, pp 158–207
Eaton-Mordas CA, Moore KG (1978) Seed glycoproteins of Lupinus angustifolius. Phytochemistry 17: 619–621
El-Gharbawi M, Whitaker JR (1963) Fractionation and partial characterization of the proteolytic enzymes of stem bromelain. Biochemistry 2: 476–481
Englund PT, King TP, Craig LC, Walti A (1968) Studies on Ficin. 1. Its isolation and characterization. Biochemistry 7: 163–175
Ericson MC, Chrispeels MJ (1973) The isolation and characterization of glucosamine- containing storage glycoproteins from the cotyledons of Phaseolus aureus. Plant Physiol 52: 98–104
Ericson MC, Chrispeels MJ (1976) The carbohydrate moiety of mung bean vicilin. Aust J Plant Physiol 3: 763–769
Esquerré-Tugayé MT, Lamport DTA (1979) Cell surface in plant-microorganism interactions. 1. A structural investigation of cell wall hydroxyproline-rich glycoprotein which accumulate in fungus infected plants. Plant Physiol 64: 314–319
Esquerré-Tugayé MT, Mazau D (1974) Effect of fungal disease on extensin, the plant cell wall glycoprotein. J Exp Bot 25: 509–513
Etzler ME, Kabat EA (1970) Purification and characterization of a lectin (plant hemagglutinin) with blood group A specificity from Dolichos biflorus. Biochemistry 9: 869–877
Eylar EH (1965) On the biological role of glycoproteins. J Theoret Biol 10: 89–113
Faye L, Berjonneau C (1979) Evidence for the glycoprotein nature of radish β-fructosidase. Biochimie 61: 51–59
Feeney RE, Yeh Y (1978) Antifreeze proteins from fish bloods. Adv Protein Chem 32: 191–282
Feinstein G, Whitaker JR (1964) On the molecular weight of the proteolytic enzymes of stem bromelain. Biochemistry 3: 1050–1054
Felker P, Bandurski RS (1975) Quantitative gas-liquid chromatography and mass spectrometry of the N(0)-perfluorobutyryl-O-isoamyl derivatives of amino acids. Anal Biochem 67: 245–262
Fincher GB, Stone BA (1974) A water-soluble arabinogalactanpeptide from wheat endosperm. Aust J Biol Sci 27: 117–132
Fincher GB, Sawyer WH, Stone BA (1974) Chemical and physical properties of an arabino-galactan-peptide from wheat endosperm. Biochem J 139: 535–545
Foriers A, Driessche Van E, Neve De R, Kanarek L, Strosberg AD (1977) The subunit structure and N-terminal sequences of the α- and β-subunits of the lentil lectin (Lens culinaris). FEBS Lett 75: 237–240
Foriers A, Neve De R, Kanarek L, Strosberg AD (1978) Common ancestor for concanavalin A and lentil lectin? Proc Natl Acad Sci USA 75: 1136–1139
Friedenson B, Liener IE (1972) The active site sequence of multiple forms of ficin. Arch Biochem Biophys 149: 169–174
Friedenson B, Liener IE (1974) Evidence that ficin is a glycoprotein. Biochim Biophys Acta 342: 209–211
Funatsu M, Funatsu G, Ishiguro M, Nanno S, Hara K (1971) Structure and toxic function of ricin. II Subunit structure of ricin D. Proc Jpn Acad 47: 718–723
Galbraith W, Goldstein IJ (1970) Phytohemagglutinin: A new class of metalloproteins. Isolation, purification and some properties of the lectin from Phaseolus lunatus. FEBS Lett 9: 197–201
Galbraith W, Goldstein IJ (1972) Phytohemagglutinin of the lima bean (Phaseolus lunatus). Isolation, characterization and interaction with type A blood-group substance. Biochemistry 11: 3976–3984
Gander JE, Jentoft NH, Drewes LR, Rick PD (1974) 5-0-β-D-galactofuranosyl-containing exocellular glycopeptide of Penicillium charlesii. Characterization of the phospho-galactomannan. J Biol Chem 249: 2063–2072
Gascon S, Neumann NP, Lampen JO (1968) Comparative study of the properties of the purified internal and external invertases from yeast. J Biol Chem 243: 1573–1577
Gatehouse JA, Croy RRD, Boulter D (1980) Isoelectric-focusing properties and carbohydrate content of pea (Pisum sativum) legumin. Biochem J 185: 497–503
Gleeson PA, Clarke AE (1979) Structural studies on the major component of Gladiolus style mucilage, an arabinogalactan-protein. Biochem J 181: 607–621
Gleeson PA, Jermyn MA, Clarke AE (1979) Isolation of an arabino-galactan protein by affinity chromatography on tridacnin-Sepharose 4B. Anal Biochem 92: 41–45
Glossman H, Neville DM (1971) Glycoproteins of cell surfaces. A comparative study of three different cell surfaces of the rat. J Biol Chem 146: 6339–6346
Goldstein I J, Hayes CE (1978) The lectins: carbohydrate-binding proteins of plants and animals. In: Tipson RS, Horton D (eds) Advances in carbohydrate chemistry and biochemistry, vol XXXV. Academic Press, London New York, pp 127–340
Gordon JA, Blumberg S, Lis H, Sharon N (1972) Purification of soybean agglutinin by affinity chromatography on Sepharose-N-E-amino-caproyl-β-galactopyranosylamine. FEBS Lett 24: 193–196
Gotelli IB, Cleland R (1968) Differences in the occurrence and distribution of hydroxyproline-proteins among the algae. Am J Bot 55: 907–914
Gottschalk A ( 1972 a) Definition of glycoproteins and their delineation from other carbohydrate-protein complexes. In: Gottschalk A (ed) Glycoproteins: Their composition, structure and function, 2nd edn, part A. Elsevier, Amsterdam, pp 24–30
Gottschalk A (ed) (1972b) Glycoproteins: Their composition, structure and function, 2nd edn, parts A, B. Elsevier, Amsterdam
Gould NR, Scheinberg SL (1970 a) Isolation and partial characterization of two anti-A hemagglutinins from P. lunatus. Arch Biochem Biophys 137: 1–11
Gould NR, Scheinberg SL (1970 b) Involvement of sulphydryl groups in the activity of anti-A hemagglutinin of Phaseolus lunatus. Arch Biochem Biophys 141: 607–613
Grant JR, Lawrence JM (1964) Effects of sodium dodecyl sulphate and other dissociating reagents on the globulins of peas. Arch Biochem Biophys 108: 522–561
Green JR, Northcote DH (1978) The structure and function of glycoproteins synthesized during slime-polysaccharide production by membranes of the root cap cells of maize (Zea mays). Biochem J 170: 599–608
Gum EK, Brown RD (1976) Structural characterization of a glycoprotein cellulase, l,4-β-D- glucan cellobiohydrolase C, from Trichoderma viride. Biochim Biophys Acta 446: 371–386
Hapner KD, Robbins JE (1979) Isolation and properties of a lectin from sainfoin (Onobrychis viciifolia, scop). Biochim Biophys Acta 580: 186–197
Hara K, Ishiguro M, Funatsu G, Funatsu M (1974) An improved method for the purification of ricin D. Agrie Biol Chem 38: 65–70
Hara K, Ishiguro M, Funatsu G, Funatsu M (1975 a) Physical, chemical and physiological properties of S-carboxymethyl subunits of ricin D. Agric Biol Chem 39: 1631–1637
Hara K, Ishiguro M, Funatsu G, Funatsu M (1975 b) Structure-toxicity relationship in subunit structure of ricin D. Agric Biol Chem 39: 1639–1644
Hasegawa K, Kusano T, Mitsuda H (1963) Fractionation of soybean proteins by gel filtration. Agrie Biol Chem 27: 878–890
Hasilik A, Tanner W (1978) Carbohydrate moiety of carboxypeptidase Y and perturbation of its biosynthesis. Eur J Biochem 91: 567–575
Hawker JS (1969) Insoluble invertases from grapes: An artefact of extraction. Phytochemistry 8: 337–344
Hayes CE, Goldstein IJ (1974) An α-D-galactosyl-binding lectin from Bandeiraea simplificola seeds. Isolation by affinity chromatography and characterization. J Biol Chem 249: 1904–1914
Hayes ML, Castellino FJ ( 1979 a) Carbohydrate of the human plasminogen variants. I. Carbohydrate composition, glycopeptide isolation and characterization. J Biol Chem 254: 8768–8771
Hayes ML, Castellino FJ ( 1979 b) Carbohydrate of the human plasminogen variants. II. Structure of the asparagine-linked oligosaccharide unit. J Biol Chem 254: 8772–8776
Heaney-Kieras J, Rodén L, Chapman DJ (1977) The covalent linkage of protein to carbohydrate in the extracellular protein-polysaccharide from the red alga Porphyridium cruentum. Biochem J 165: 1–9
Heath MF, Northcote DH (1971) Glycoprotein of the wall of sycamore tissue-culture cells. Biochem J 125: 953–961
Heinicke RM, Gortner WA (1957) Stem bromelain - A new protease preparation from pineapple plants. Econ Bot 11: 225–234
Hemming FW (1977) Dolichol phosphate, a coenzyme in the glycosylation of animal membrane-bound glycoproteins. Biochem Soc Trans 5: 1223–1231
Hemming FW (1978) Polyprenyl phosphates as coenzymes in protein and oligosaccharide glycosylation. Philos Trans R Soc London Ser B 284: 559–568
Hillestad A, Wold JK (1977) Water-soluble glycoproteins from Cannabis sativa ( South Africa ). Phytochemistry 16: 1947–1951
Hillestadt A, Wold JK, Paulsen BS (1977) Structural studies of water-soluble glycoproteins from Cannabis sativa. Carbohydr Res 57: 135–144
Hills GJ, Phillips JM, Gay MR, Roberts K (1972) Structure, composition and morphogenesis of the cell wall of Chlamydomonas reinhardii. J Ultrastruct Res 40: 599–613
Homer RB, Roberts K (1979) Glycoprotein conformation in plant cell walls. Circular dichroism reveals a polyproline 11 structure. Planta 146: 217–222
Hopp HE, Romero PA, Daleo GR, Pont Lezica R (1978) Biosynthesis of cellulose precursors. The involvement of lipid-linked sugars. Eur J Biochem 84: 561–571
Horejsi V, Kocourek J (1978) Studies on lectins. XXXVII. Isolation and characterization of the lectin from Jimson-weed seeds (Datura stramonium L). Biochim Biophys Acta 532: 92–97
Hori H, Fujii T (1978) Intracellular hydroxyproline-rich glycoproteins of the suspension-cultured tobacco cells. Plant Cell Physiol 19: 1271–1280
Hori H, Sato S (1977) Extracellular hydroxyproline-rich glycoprotein of suspension-cultured tobacco cells. Phytochemistry 16: 1485–1487
Howard IK, Sage HJ, Stein MD, Young NM, Leon MA, Dyckers DF (1971) Studies on a phytohemagglutinin from the lentil. II Multiple forms of Lens culinaris hemagglutinin. J Biol Chem 246: 1590–1595
Hughes RC (1976) Membrane glycoproteins. A review of structure and function. Butterworths, London
Hunkapiller MW, Hood LE (1978) Direct microsequence analysis of polypeptides using an improved sequencator, a nonprotein carrier (polybrene), and high pressure liquid chromatography. Biochemistry 17: 2124–2133
Ishiguro M, Takahashi T, Funatsu G, Hayashi K, Funatsu M (1964) Biochemical studies on ricin. I Purification of ricin. J Biochem (Tokyo) 55: 587–592
Ishihara H, Takahashi N, Oguri S, Tejima S (1979) Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides. J Biol Chem 254: 10715–10719
Jackoby WB (ed) (1971) Methods in enzymology, vol XXII. Academic Press, London New York, pp 273–437
Jackson P, Boulter D, Thurman DA (1969) A comparison of some properties of vicillin and legumin isolated from seeds of Pisum sativum, Vicia faba and Cicer arietinum. New Phytol 68: 25–33
Jackson RL, Hirs CHW (1970) The primary structure of porcine pancreatic ribonuclease. I. The distribution and sites of carbohydrate attachment. J Biol Chem 245: 624–636
Jaffe WG, Hannig K (1965) Fractionation of proteins from kidney beans (Phaseolus vulgaris). Arch Biochim Biophys 109: 80–91
Jamieson GA (1965) Studies on glycoproteins. I. The carbohydrate portion of human ceruloplasmin. J Biol Chem 240: 2019–2027
Jaynes TA, Nelson OE (1971) Invertase activity in normal and mutant maize endosperms during development. Plant Physiol 47: 623–628
Jennings AC (1978) The hexosamine content of some seeds and pollens. J Sci Food Agric 29: 915–924
Jennings AC, Pusztai A, Synge RLM, Watt WB (1968) Fractionation of plant material. III - two schemes for chemical fractionation of fresh leaves, having special applicability for isolation of bulk protein. J Sci Food Agric 19: 203–213
Jermyn MA, Yeow YM (1975) A class of lectins present in the tissues of seed plants. Aust J Plant Physiol 2: 501–531
Johansen PG, Marshall RD, Neuberger A (1960) Carbohydrates in protein. 2. The hexose, hexosamine, acetyl and amide nitrogen contents of hens-egg albumin. Biochem J 77: 239–247
Jones IK, Glazer AN (1970) Comparative studies on four sulphydryl endopeptidases (“ficins”) of Ficus glabrata latex. J Biol Chem 245: 2765–2772
Kabat EA, Heidelberger M, Bezer AR (1947) A study of the purification and properties of ricin. J Biol Chem 168: 629–639
Kärkkäinen J (1970) Analysis of disaccharides as permethylated dissacharide alditols by gas-liquid chromatography-mass spectrometry. Carbohydr Res 14: 27–33
Kärkkäinen J (1971) Structural analysis of trisaccharides as permethylated methyl glycosides by gas-liquid chromatography-mass spectrometry. Carbohydr Res 17: 1–10
Karr AL (1972) Isolation of an enzyme system which will catalyze the glycosylation of extensin. Plant Physiol 50: 275–282
Keegstra K, Talmadge KW, Bauer WD, Albersheim P (1973) The structure of plant cell walls. III. A model of the walls of suspension-cultured sycamore cells based on the interconnections of the macromolecular components. Plant Physiol 51: 188–197
King NJ, Bayley ST (1965) A preliminary analysis of the protein of the primary cell walls of some plant cells. J Exp Bot 16: 294–303
King TP, Norman PS (1962) Isolation studies of allergens from ragweed pollen. Biochemistry 1: 709–720
Klapper MH, Hackett DP (1965) Investigations on the multiple components of commercial horseradish peroxidase. Biochim Biophys Acta 96: 272–282
Knee M (1975) Soluble and wall bound glycoproteins of apple fruit tissue. Phytochemistry 14: 2181–2188
Kornfeld R, Kornfeld S (1970) The structure of a phytohemagglutinin receptor site from human erythrocytes. J Biol Chem 245: 2536–2545
Kornfeld R, Kornfeld S (1976) Comparative aspects of glycoprotein structure. Annu Rev Biochem 45: 217–237
Koshiyama I (1965) Purification of the 7S component of soybean proteins. Agric Biol Chem 29: 885–887
Koshiyama I (1968 a) Chemical and physical properties of a 7S protein in soybean globulins. Cereal Chem 45:394–404
Koshiyama I (1968 b) Chromatographic and sedimentation behaviours of a purified 7S protein in soybean globulins. Cereal Chem 45:405–412
Koshiyama I (1969) Isolation of a glycopeptide from a 7S protein in soybean globulins. Arch Biochem Biophys 130: 370–373
Koshiyama I (1971) Subunit structure of a 7S protein in soybean globulins. Agric Biol Chem 35: 385–392
Koshiyama I, Fukushima D (1976 a) Identification of the 7S globulin with β-conglycinin in soybean seeds. Phytochemistry 15: 157–159
Koshiyama I, Fukushima D (1976 b) Purification and some properties of α-conglycinin in soybean seeds. Phytochemistry 15: 161–164
Krammer DE, Whitaker JR (1969) Multiple molecular forms of ficin - evidence against autolysis as explanation. Plant Physiol 44: 1560–1565
Kuhn RW, Walsh KA, Neurath (1974) Isolation and partial characterization of an acid carboxypeptidase from yeast. Biochemistry 13: 3871–3877
Lamport DTA (1965) The protein component of primary cell walls. In: Preston RD (ed) Advances in botanical research, vol II. Academic Press, New York London, pp 151–218
Lamport DTA (1967) Hydroxyproline-O-glycosidic linkage of the plant cell wall glycoprotein extensin. Nature (London) 216: 1322–1324
Lamport DTA (1969) The isolation and partial characterization of hydroxyproline-rich glycopeptides obtained by enzymic degradation of primary cell walls. Biochemistry 8: 1155–1163
Lamport DTA, Miller DH (1971) Hydroxyproline arabinosides in the plant kingdom. Plant Physiol 48: 454–456
Lamport DTA, Northcote DH (1960) Hydroxyproline in primary cell walls of higher plants. Nature (London) 188: 665–666
Lamport DTA, Katona L, Roerig S (1973) Galactosylserine in extensin. Biochem J 133: 125–131
Lee YC, Scocca JR (1972) A common structural unit in asparagine-oligosaccharides of several glycoproteins from different sources. J Biol Chem 247: 5753–5758
Lehle L, Cohen RE, Ballou CE (1979) Carbohydrate structure of yeast invertase. Demonstration of a form with only core oligosaccharides and a form with completed polysaccharide chains. J Biol Chem 254: 12209–12218
Liener IE (1976) Phytohemagglutinins (phytolectins). Annu Rev Plant Physiol 28: 291–319
Liener IE, Pallansch (1952) Purification of a toxic substance from defatted soybean flour. J Biol Chem 197: 29–36
Lin J-Y, Tserng K-Y, Chen C-C, Tung T-C (1970) Abrin and ricin: New anti-tumor substances. Nature (London) 227: 292–293
Lin J-Y, Liu K, Chen C-C, Tung T-C (1971) Effect of crystalline ricin on the biosynthesis of protein, RNA and DNA in experimental tumor cells. Cancer Res 31: 921–924
Lin J-Y, Pao C-C, Ju S-T, Tung C-C (1972) Polyribosome disaggregation in rat following administration of the phytotoxic proteins, abrin and ricin. Cancer Res 32: 943–947
Lis H, Sharon N (1973) The biochemistry of plant lectins (phytohemagglutinins). Annu Rev Biochem 42: 541–574
Lis H, Sharon N (1978) Soybean agglutinin - A plant glycoprotein. Structure of the carbohydrate unit. J Biol Chem 253: 3468–3476
Lis H, Sharon N, Katchalski E (1964) Isolation of a mannose-containing glycopeptide from soybean hemagglutinin. Biochim Biophys Acta 83: 376–378
Lis H, Fridman C, Sharon N, Katchalski E (1966a) Multiple hemagglutinins in soybean. Arch Biochim Biophys 117: 301–309
Lis H, Sharon N, Katchalski E (1966b) Soybean hemagglutinin, a plant glycoprotein, I. Isolation of a glycopeptide. J Biol Chem 241: 684–689
Lis H, Sharon N, Katchalski E(1969) Identification of the carbohydrate-protein linkage group in soybean hemagglutinin. Biochim Biophys Acta 192: 364–366
Lis H, Sela B-A, Sachs L, Sharon N (1970) Specific inhibition by N-acetyl-D-galactosamine of the interaction between soybean agglutinin and animal cell surfaces. Biochim Biophys Acta 211: 582–585
Liu EH, Lamport DTA (1974) An accounting of horseradish peroxidase isozymes associated with the cell wall and evidence that peroxidase does not contain hydroxyproline. Plant Physiol 54: 870–876
Loomis WD, Battaile J (1966) Plant phenolic compounds and the isolation of plant enzymes. Phytochemistry 5: 423–438
Lotan R, Siegelman HW, Lis H, Sharon N (1974) Subunit structure of soybean agglutinin. J Biol Chem 249: 1219–1224
Lotan R, Debray H, Cacan M, Cacan R, Sharon N (1975) Labelling of soybean agglutinin by oxidation with sodium periodate followed by reduction with sodium [3H] borohydride. J Biol Chem 250: 1955–1957
Mani UV, Radhakrishnan AN (1974) Isolation and characterization of a hydroxyproline- containing protein from the soluble extracts of the leaves of Sandal (Santalum album L). Biochem J 141: 147–153
March JF (1975) A modified technique for the quantitative analysis of amino acids by gas chromatography using heptafluorobutyric n-propyl derivatives. Anal Biochem 69: 420–442
Marinkovich VA (1964) Purification and characterization of the hemagglutinin present in potatoes. J Immunol 93: 732–741
Marshall RD (1972) Glycoproteins. Annu Rev Biochem 41: 673–702
Marshall RD (1979 a) Some observations on why many proteins are glycosylated. Biochem Soc Trans 7:800–805
Marshall RD (1979b) Structures and functions of Glycoproteins. In: Offord RE (ed) Chemistry of macromolecules, IIB macromolecular complexes. International review of biochemistry, vol XXV. Univ Park Press, Baltimore, pp 1–53
Marshall RD, Neuberger A (1970) Aspects of the structure and metabolism of glycoproteins. In: Tipson RS, Horton D (eds) Advances in carbohydrate chemistry and biochemistry, vol XXV. Academic Press, London New York, pp 407–478
Marshall RD, Neuberger A (1972) Qualitative and quantitative analysis of the component sugars. In: Gottschalk A (ed) Glycoproteins: Their composition, structure and function, 2nd edn, part A. Elsevier, Amsterdam, pp 224–229
Matsumoto I, Osawa T (1969) Purification and characterization of an anti-H(O) phytohemagglutinin of Ulex europaeus. Biochim Biophys Acta 194: 180–189
Matsumoto I, Osawa T (1970) Purification and characterization of a cystisus-type anti-H(O) phytohemagglutinin from Ulex europaeus. Arch Biochem Biophys 140: 484–491
Mazza G, Charles C, Bouchet M, Richard J, Raynoud J (1968) Isolement, purification et properties physico-chemiques des peroxydase de navat. Biochim Biophys Acta 167: 89–98
Mazza G, Job C, Bouchet M (1973) Chemical composition and hydrodynamic characteristics of turnip peroxidase. Biochim Biophys Acta 322: 218–223
McKerrow JH, Robinson AB (1971) Deamidation of asparaginyl residues as a hazard in experimental protein and peptide procedures. Anal Biochem 42: 565–568
McNamara MK, Stone BA (1978) Isolation of a carbohydrate-protein linkage compound from wheat endosperm arabinogalactanpeptide and its chemical synthesis. In: International union of pure and applied chemists. IX Int Symp Carbohydr Chem Abstr A15: 43
Mescher MF, Strominger JL (1976) Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium. J Biol Chem 251: 2005–2014
Miller DH, Lamport DTA, Miller M (1972) Hydroxyproline hetero-oligosaccharides in Chlamydomonas. Science 176: 918–920
Minobe S, Nakayima H, Hoh N, Funakeshi I, Yamashina I (1979) Structure of a major oligosaccharide of Taka-amylase A. J Biochem (Tokyo) 86: 1851–1854
Misaki A, Goldstein IJ (1977) Glycosyl moiety of the lima bean lectin. J Biol Chem 252: 6995–6999
Monro J A, Bailey RW, Penny D (1976 a) Hemicellulose fraction and associated protein of lupin hypocotyl cell walls. Phytochemistry 15: 175–181
Monro JA, Penny D, Bailey RW (1976 b) The organization and growth of primary cell walls of lupin hypocotyl. Phytochemistry 15: 1193–1198
Montgomery R (1970) Glycoproteins. In: Pigman W, Horton D (eds) The carbohydrates, chemistry and biochemistry, vol IIB, Academic Press, London New York, pp 628–709
Montgomery R, Wu Y-C (1963) The carbohydrate of ovomucoid. Isolation of glycopeptides and the carbohydrate-protein linkage. J Biol Chem 238: 3547–3554
Morris HR, Williams DH, Ambler RP (1971) Determination of the sequences of protein- derived peptides and peptide mixtures by mass spectrometry. Biochem J 125: 189–201
Mort AJ (1978) Partial characterization of extensin by selective degradation of cell walls. PhD Thesis, Michigan State Univ, USA
Mort AJ, Lamport DTA (1977) Anhydrous hydrogen fluoride deglycosylates glycoproteins. Anal Biochem 82: 289–309
Muir L, Lee YC (1969) Structure of the D-galactose oligosaccharides from earthworm cuticle collagen. J Biol Chem 244: 2343–2349
Murachi T (1964) Amino acid composition of stem bromelain. Biochemistry 3: 932–934
Murachi T, Neurath H (1960) Fractionation and specificity studies on stem bromelain. J Biol Chem 235: 99–107
Murachi T, Yasui M, Yasuda Y (1964) Purification and physical characterization of stem bromelain. Biochemistry 3: 48–55
Murachi T, Suzuki A, Takahashi N (1967) Evidence for glycoprotein nature of stem bromelain. Isolation of a glycopeptide. Biochemistry 6: 3730–3736
Murray RHA (1978) Potato lectin. PhD Thesis, Cambridge Univ, UK
Murray RHA, Northcote DH (1978) Oligoarabinosides of hydroxyproline isolated from potato lectin. Phytochemistry 17: 623–629
Namen AE, Hapner KD (1979) The glycosyl moiety of lectin from sainfoin (Onobrychis viciifolia, scop). Biochim Biophys Acta 580: 198–209
Nanno S, Ishiguro M, Funatsu G, Funatsu M (1975 a) Isolation of glycopeptides from ricin D. Agric Biol Chem 39: 1645–1650
Nanno S, Ishiguro M, Funatsu G, Funatsu M (1975 b) The mode of binding of carbohydrate in ricin D. Agric Biol Chem 39: 1651–1654
Nash AM, Wolf WF (1967) Solubility and ultracentrifugal studies on soybean globulins. Cereal Chem 44: 183–192
Nash AM, Kwolek WF, Wolf WJ (1974) Extraction of soybean proteins with aqueous 2-mercaptoethanol. Cereal Chem 51: 220–227
Neuberger A (1938) Carbohydrate in proteins. I. The carbohydrate component of crystalline egg albumin. Biochem J 32: 1435–1451
Neuberger A, Gottschalk A, Marshall RD, Spiro RG (1972) Carbohydrate-peptide linkages in glycoproteins and methods for their elucidation. In: Gottschalk A (ed) Glycoproteins: Their composition, structure and function, 2nd, edn, part A. Elsevier, Amsterdam, pp 450–490
Neumann P, Lampen JO (1969) The glycoprotein structure of yeast invertase. Biochemistry 8: 3552–3556
Nicolson GL, Blaustein J, Etzler ME (1974) Characterization of two plant lectins from Ricinus communis and their quantitative interaction with murine lymphoma. Biochemistry 13: 196–204
Northcote DH (1972) Chemistry of the plant cell wall. Annu Rev Plant Physiol 23: 113–132
Northcote DH (1979) The involvement of the golgi apparatus in the biosynthesis and secretions of glycoproteins and polysaccharides. In: Manson LA (ed) Biomembranes, vol X. Plenum Publ Co, New York, pp 51–76
Nozaki Y, Tanford C (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J Biol Chem 246: 2211–2217
O’Dell BL, De Boland A (1976) Complexation of phytate with protein and cations in corn germ and cations in corn germ and oilseed meals. J Agric Food Chem 24: 804–808
Oh YA, Conrad RA (1971) Some properties of mitogenic components isolated from phytohemagglutinin by a preparative gel electrophoresis. Arch Biochem Biophys 146: 525–530
Okabayashi H, Isemura T, Sakakibara S (1968) Steric structure of L-proline oligopeptides. II. Far ultraviolet absorption spectra and optical rotations of L-proline oligopeptides. Biopolymers 6: 323–330
Olsnes S, Phil A ( 1972 a) Ricin. Potent inhibitor of protein synthesis. FEBS Lett 20: 327–329
Olsnes S, Phil A ( 1972 b) Treatment of abrin and ricin with β-mercaptoethanol. Opposite effects on their toxicity in mice and their ability to inhibit protein synthesis in a cell free system. FEBS Lett 28: 48–50
O’Neill MA, Roberts K (1981) Methylation analysis of cell wall glycoproteins and glycopeptides from Chlamydomonas reinhardii. Phytochemistry 20: 25–28
O’Neill MA, Selvendran RR (1980) Glycoproteins from the cell wall of Phaseolus coccineus. Biochem J 187: 53–63
Osbourne DJ, Ridge I (1971) Role of peroxidase when hydroxyproline-rich protein in plant cell walls is increased by ethylene. Nature (London) 229: 205–208
Osbourne TB, Campbell GF (1898) Proteids of the pea. J Am Chem Soc 20: 348–362
Ota S (1968) Autodigestion of the main proteolytically active component of the stem bromelain. J Biochem (Tokyo) 63: 494–500
Ota S, Moore S, Stein WH (1964) Preparation and chemical properties of purified stem and fruit bromelain. Biochemistry 3: 180–185
Pallansch MJ, Liener IE (1953) Soyin, a toxic protein from the soybean. II. Physical characterization. Arch Biochem Biophys 45: 366–374
Parodi AJ, Leloir LF (1979) The role of lipid intermediates in the glycosylation of proteins in the eukaryotic cell. Biochim Biophys Acta 559: 1–37
Paul KG (1958) Isolation of horseradish peroxidase. Acta Chem Scand 12: 1312–1318
Pazur JH, Kleppe K, Cepure A (1965) A glycoprotein structure for glucose oxidase from Aspergillus niger. Arch Biochem Biophys 111: 351–357
Pazur JH, Knull HR, Simpson DL (1970) Glycoenzymes: role for the carbohydrate moieties. Biochem Biophys Res Commun 40: 110–116
Pearce RJ (1977) Amino acid analysis by gas-liquid chromatography of N-heptafluorobutyryl isobutyl esters. J Chromatogr 136: 113–126
Peisach J, Levine WG, Blumberg WE (1967) Structural properties of stellacyanin, a copper containing mucoprotein from Rhus vernicifera, the Japanese lac tree. J Biol Chem 242: 2847–2858
Pereira MEA, Kabat EA, Sharon N (1974) Immunochemical studies on the specificity of soybean agglutinin. Carbohydr Res 37: 89–102
Phelps C, Forlani L, Antonini E (1971) The hydrogen ion equilibria of horseradish peroxidase and apoperoxidase. Biochem J 124: 605–614
Plummer TH, Hirs CHW (1964) On the structure of bovine ribonuclease B. Isolation of a glycopeptide. J Biol Chem 239: 2530–2538
Pont Lezica R (1979) Glycosylation of glycoproteins in green plants and algae. Biochem Soc Trans 7: 334–337
Pope DG (1977) Relationship between hydroxyproline-containing proteins secreted into the cell wall and medium by suspension cultured Acer pseudoplatanus cells. Plant Physiol 59: 894–900
Poretz RD, Riss H, Timberlake JW, Chien S-M (1974) Purification and properties of the hemagglutinin from Sophora japonica seeds. Biochemistry 13: 250–256
Prentice N, Robbins GS (1976) Composition of invertases from germinated barley. Cereal Chem 53: 874–880
Preston RD (1979) Polysaccharide conformation and cell wall function. Annu Rev Plant Physiol 30: 55–78
Puski G, Melnychyn P (1968) Starch-gel electrophoresis of soybean globulins. Cereal Chem 45: 192–201
Pusztai A (1964) Hexosamine in the seeds of higher plants (spermatophytes). Nature (London) 201: 1328–1329
Pusztai A (1965a) A study of the glucosamine containing constituents of the seeds of kidney bean (Phaseolus vulgaris). Biochem J 94: 604–610
Pusztai A (1965 b) Studies on the extraction of nitrogenous and phosphorus containing materials from the seeds of the kidney bean (Phaseolus vulgaris). Biochem J 94:611–616
Pusztai A (1965 c) The isolation and characterization of a glycoprotein from the seeds of kidney beans. Biochem J 95: 3c–5c
Pusztai A (1966 a) Interaction of proteins with other polyelectrolytes in a two-phase system containing phenol and aqueous buffers at various pH values. Biochem J 99:93–101
Pusztai A (1966 b) The isolation of two proteins, glycoprotein I and a trypsin inhibitor from the seeds of kidney bean (Phaseolus vulgaris). Biochem J 101:379–384
Pusztai A, Ducan I (1971) Glycoprotein - I of Phaseolus vulgaris - homogeneity and enzymic properties. Biochim Biophys Acta 229: 785–794
Pusztai A, Watt WB (1969) Fractionation and characterization of glycoproteins containing hydroxyproline from the leaves of Vicia faba. Eur J Biochem 10: 523–532
Pusztai A, Watt WB (1970) Glycoprotein II. The isolation and characterization of a major antigenic and non-hemagglutinating glycoprotein from Phaseolus vulgaris. Biochim Biophys Acta 207: 413–431
Pusztai A, Begbie R, Duncan I (1971) Fractionation and characterization of water-soluble polysaccharide-protein complexes containing hydroxyproline from the leaves of Vicia faba. J Sci Food Agric 22: 514–519
Pusztai A, Croy RRD, Grant G, Watt WB (1977) Compartmentalization in the cotyledonary cells of Phaseolus vulgaris L. seeds: A differential sedimentation study. New Phytol 79: 61–71
Rackis J J, Sasame HA, Anderson RL, Smith AK (1959) Chromatography of soybean proteins. I. Fractionation of whey proteins in diethyl-aminoethyl-cellulose. J Am Chem Soc 81: 6265–6270
Racusen D, Foote M (1971) The major glycoproteins in germinating bean seeds. Can J Bot 49: 2107–2111
Rees MW, Short MN, Self R, Eagles J (1974) The amino acid sequences of the tryptic peptides of the cowpea strain of tobacco mosaic virus protein. Biomed Mass Spec 1: 237–251
Reinhold VN, Dunne FT, Wriston JC, Schwarz M, Sarda L, Hirs CHW (1968) The isolation of porcine ribonuclease, a glycoprotein from pancreatic juice. J Biol Chem 243: 6482–6494
Reisfeld RA, Börjeson J, Chessin LN, Small PA (1967) Isolation and characterization of a mitogen from pokeweed (Phytolacca americana). Proc Natl Acad Sci USA 58: 2020–2027
Riordan JF, Valle BF (1972) Reactions with N-ethylmaleimide and p-mercuribenzoate. In: Hirs CHW, Timasheff SN (eds) Methods in enzymology, vol XXV. Academic Press, London New York, pp 449–456
Robbins PW (1979) Glycosylation of viral glycoproteins by host animal cells. Biochem Soc Trans 7: 320–322
Roberts K (1979) Hydroxyproline: Its assymmetric distribution in a cell wall glycoprotein. Planta 146: 275–279
Roberts K, Northcote DH (1972) Hydroxyproline: Observations on its chemical and autoradiographic localization in plant cell walls. Planta 107: 43–51
Roberts K, Gurney-Smith M, Hills GJ (1972) Structure, composition and morphogenesis of the cell wall of Chlamydomonas reinhardii. J Ultrastruct Res 40: 599–613
Roberts RC, Briggs DR (1965) Isolation and characterization of the 7S component of soybean globulins. Cereal Chem 42: 71–85
Roberts RM, Connor AB, Cetorelli JJ (1971) The formation of glycoproteins in tissues of higher plants. Specific labelling with D-[1-14C-] glucosamine. Biochem J 125: 999–1008
Roberts RM, Cetorelli J J, Kirby EG, Ericson M (1972) Location of glycoproteins that contain glucosamine in plant tissue. Plant Physiol 50: 531–535
Rodén L (1970) Structure and metabolism of the proteoglycans of chondroitin sulphate and keratan sulphate. In: Balazs EA (ed) Chemistry and molecular biology of the intercellular matrix (Advanced Study Institute). Academic Press, London New York, pp 797–821
Rosario Del EJ, Santisopasri V (1977) Characterization and inhibition of invertases in sugar cane juice. Phytochemistry 16: 443–445
Roseman S (1970) The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion. Chem Phys Lipids 5: 270–297
Sacher JA (1966) The regulation of sugar uptake and accumulation in bean pod tissue. Plant Physiol 41: 181–189
Sadava D, Chrispeels MJ (1978) Synthesis and secretion of cell wall glycoproteins in carrot root discs. In: Khal G (ed) Biochemistry of wounded plant tissues. DeGryter, Berlin New York, pp 85–102
Scocca J, Lee YC (1969) The composition and structure of the carbohydrate of pineapple stem bromelain. J Biol Chem 244: 4852–4863
Sela B-A, Lis H, Sharon N, Sachs L (1973) Isolectins from wax bean with differential agglutination of normal and transformed mammalian cells. Biochim Biophys Acta 310: 273–277
Selvendran RR (1975a) Analysis of cell wall material from plant tissues: extraction and purification. Phytochemistry 14: 1011–1017
Selvendran RR (1975b) Cell wall glycoproteins and polysaccharides of parenchyma of Phaseolus coccineus. Phytochemistry 14: 2175–2180
Selvendran RR, Davies AMC, Tidder E (1975) Cell wall glycoproteins and polysaccharides of mature runner beans. Phytochemistry 14: 2169–2174
Shannon LM (1968) Plant isoenzymes. Annu Rev Plant Physiol 19: 187–210
Shannon LM, Kay E, Lew JY (1966) Peroxidase isoenzymes from horseradish roots. I. Isolation and physical properties. J Biol Chem 241: 2166–2172
Sharma CB, Babczinski P, Lehle L, Tanner W (1974) The role of dolicholmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae. Eur J Biochem 46: 35–41
Sharon N (1974) Glycoproteins of higher plants. In: Pridham JB (ed) Plant carbohydrate biochemistry. Academic Press, London New York, pp 235–252
Sharon N, Lis H (1972) Lectins: cell-agglutinating and sugar specific proteins. Science 177: 949–959
Sharon N, Lis H (1979) Comparative biochemistry of plant glycoproteins. Biochem Soc Trans 7: 783–799
Shih HC, Shannon LM, Kay E, Lew JY (1971) Peroxidase isoenzymes from horseradish roots. IV Structural relationships. J Biol Chem 246: 4546–4551
Smellie RMS, Beeley JG (eds) (1974) The metabolism and function of glycoproteins. Biochem Soc Symp 40: 1–189
Smith AK, Rackis J J (1957) Phytin elimination in soybean protein isolation. J Am Chem Soc 79: 633–637
Spiro RG (1967) Studies on the renal glomerular basement membrane. Nature of the carbohydrate units and their attachment to the peptide portion. J Biol Chem 242: 1923–1932
Spiro RG (1969) Characterization and quantitative determination of the hydroxylysine-linked carbohydrate units of several collagens. J Biol Chem 244: 602–612
Spiro RG (1970) Glycoproteins. Annu Rev Biochem 39: 599–638
Spiro RG (1972) Basement membranes and collagens. In: Gottschalk A (ed) Glycoproteins: Their composition, structure and function, 2nd edn, part B. Elsevier, Amsterdam, pp 964–999
Spiro RG (1973) Glycoproteins. Adv Protein Chem 27: 350–467
Spiro RG, Fukushi S (1969) The lens capsule. Studies on the carbohydrate units. J Biol Chem 244: 2049–2058
Stead RH, De Muelenaere HJH, Quicke GV (1966) Trypsin inhibition, hemagglutinin, and intraperitoneal toxicity in extracts of Phaseolus vulgaris and Glycine max. Arch Biochem Biophys 113: 703–708
Sumere Van CF, Albrecht J, Dedoner A, De Poster H, Pe I (1975) Plant proteins and phenolics. In: Harbourne JB, Van Sumere CF (eds) The chemistry and biochemistry of plant proteins. Academic Press, London New York, pp 211–264
Tai T, Yamashita K, Ogatu-Arakawa M, Koide N, Muramatsu T, Iwashita S, Inoue Y, Kobata A (1975) Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J Biol Chem 250: 8569–8575
Takahashi N, Murachi T (1976) Stem bromelain. Isolation and purification; preparation and characterization of the carbohydrate portion. In: Whistler RL, Be Miller JN (eds) Methods in carbohydrate chemistry, vol VII. Academic Press, London New York, pp 175–184
Takahashi N, Yasuda Y, Kazuya M, Takashi M (1969) The amino acid sequence of glycopeptides isolated from stem bromelain. J Biochem (Tokyo) 66: 659–665
Takahashi T, Liener IE (1968) Isolation and composition of a glycopeptide from a phytohemagglutinin of Phaseolus vulgaris. Biochim Biophys Acta 154: 560–564
Takahashi T, Ramachandramurthy P, Liener IE (1967) Some physical and chemical properties of a phytohemagglutinin isolated from Phaseolus vulgaris. Biochim Biophys Acta 133: 123–133
Tandecarz J, Lavintman N, Cardini CE (1975) Biosynthesis of starch. Formation of a glucoproteic acceptor by a potato non-sedimentable preparation. Biochim Biophys Acta 399: 345–355
Tarentino AL, Malley F (1974) Purification and properties of an endo-β-N-acetylglucosaminidase from Streptomyces griseus. J Biol Chem 249: 811–817
Tarentino AL, Plummer TH, Maley F (1974) The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase II. J Biol Chem 249: 818–824
Thanh VH, Shibaski (1978) Major proteins of soybean seeds. Subunit structure of β-conglycinin. J Agric Food Chem 26: 692–695
Toyoshima S, Osawa T, Tonomura A (1970) Some properties of purified phytohemagglutinin from Sophora japonica seeds. Biochemistry 13: 250–256
Toyoshima S, Akiyama Y, Nakano K, Tonomura A, Osawa T (1971) A phytomitogen from Wisteria floribunda seeds and its interaction with human peripheral lymphocytes. Biochemistry 10: 4457–4463
Toyoshima S, Fukunda M, Osawa T (1972) Chemical nature of the receptor site for various phytomitogens. Biochemistry 11: 4000–4005
Trimble RB, Maley F (1977) Subunit structure of external invertase from Saccharomyces cerevisiae. J Biol Chem 252: 4409–4412
Valent BS, Darvill AG, McNeill M, Robertson BK, Albersheim P (1980) A general and sensitive chemical method for sequencing the glycosyl residues of complex carbohydrates. Carbohydr Res 79: 165–192
Varner JE, Schildlovsky G (1963) Intracellular distribution of proteins in pea cotyledons. Plant Physiol 38: 139–144
Vaughan D, MacDonald IR (1967) Development of soluble and insoluble invertase activity in washed storage tissue slices. Plant Physiol 42: 456–458
Vries De AL, Komatsu SK, Feeney RE (1970) Chemical and physical properties of freezing point-depressing glycoproteins from antartic fishes. J Biol Chem 245: 2901–2908
Wada S, Pallansch MJ, Liener IE (1958) Chemical composition and end groups of the soybean hemagglutinin. J Biol Chem 233: 395–400
Waechter CJ, Lennarz WJ (1976) The role of polyprenyl linked sugars in glycoprotein synthesis. Annu Rev Biochem 45: 95–112
Waldschmidt-Leitz K, Keller L (1970) Seed proteins XII. Toxin and agglutinin from Ricinus, purification and composition. Hoppe-Seyler’s Z Physiol Chem 351: 990–994
Walti A (1938) Crystalline ficin. J Am Chem Soc 60: 493
Wang FFC, Hirs CHW (1977) Influence of the heterosaccharides in porcine ribonuclease on the conformation and stability of the protein. J Biol Chem 252: 8358–8364
Wang JL, Becker JW, Reeke GN, Edelman GM (1974) Favin, a crystalline lectin from Vicia faba. J Mol Biol 88: 259–262
Wang JL, Cunningham BA, Waxdal MJ, Edelman GM (1975) The covalent and three- dimensional structure of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2. J Biol Chem 250: 1490–1502
Waxdal MJ (1974) Isolation, characterization and biological activities of five mitogens from pokeweed. Biochemistry 13: 3671–3676
Welinder KG (1976) Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7). FEBS Lett 72: 19–23
Welinder KG (1979) Amino acid sequence of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence and some structural characteristics of horseradish peroxidase C. Eur J Biochem 96: 483–502
Welinder KG, Mazza G (1975) Similarities and differences of five peroxidases from turnip and horseradish. Eur J Biochem 57: 415–424
Welinder KG, Mazza G (1977) Amino-acid sequences of heme-linked, histidine-containing peptides of five peroxidases from horseradish and turnip. Eur J Biochem 73: 353–358
Welinder KG, Smillie LB (1972) Amino acid sequence studies of horseradish peroxidase. II. Thermolytic peptides. Can J Biochem 50: 63–90
Williams DC, Whitaker JR (1969) Multiple molecular forms of Ficus glabrata ficin. Their separation and relative physical, chemical and enzymatic properties. Plant Physiol 44: 1574–1583
Winterburn PJ, Phelps CF (1972) The significance of glycosylated proteins. Nature (London) 236: 147–151
Wolf WJ (1970) Soybean proteins: Their functional, chemical and physical properties. J Agric Food Chem 18: 969–976
Wolf WJ, Briggs DR (1959) Purification and characterization of the 11S component of soybean proteins. Arch Biochem Biophys 85: 186–199
Wolf WJ, Sly DA (1965) Chromatography of soybean proteins on hydroxylapatite. Arch Biochem Biophys 110: 47–56
Yamaguchi H, Ikenaba T, Matsushima Y (1971) The complete sequence of a glycopeptide obtained from Taka-amylase A. J Biochem (Tokyo) 70: 587–594
Yamauchi F, Yamagishi T (1979) Carbohydrate sequence of a soybean 7S protein. Agric Biol Chem 43: 505–510
Yamauchi F, Kawase M, Kanbe M, Shibazaki K (1975) Separation of the β-aspartamido- carbohydrate fractions from soybean 7S protein: protein-carbohydrate linkage. Agric Biol Chem 39: 873–878
Yamauchi F, Thanh VH, Kawase M, Shibazaki K (1976) Separation of the glycopeptides from soybean 7S protein: their amino acid sequence. Agric Biol Chem 40: 691–696
Yariv J, Lis H, Katchalski E (1967) Precipitation of arabic acid and some seed polysaccharides by glycosylphenylazo dyes. Biochem J 105: 1c–3c
Yasuda Y, Takahashi N, Murachi T (1970) The composition and structure of carbohydrate moiety of stem bromelain. Biochemistry 9: 25–32
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Selvendran, R.R., O’Neill, M.A. (1982). Plant Glycoproteins. In: Loewus, F.A., Tanner, W. (eds) Plant Carbohydrates I. Encyclopedia of Plant Physiology, vol 13 / A. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68275-9_13
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