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Structure of Glycoproteins and Their Oligosaccharide Units

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Book cover The Biochemistry of Glycoproteins and Proteoglycans

Abstract

The presence of oligosaccharide chains covalently attached to the peptide backbone is the feature that distinguishes glycoproteins from other proteins and accounts for some of their characteristic physical and chemical properties. Glycoproteins occur in fungi, green plants, viruses, bacteria, and in higher animal cells where they serve a variety of functions. Connective tissue glycoproteins, such as the collagens and proteoglycans of various animal species, are structural elements as are the cell wall glycoproteins of yeasts and green plants. The submaxillary mucins and the glycoproteins in the mucous secretions of the gastrointestinal tract, which consist of numerous oligosaccharide chains attached at closely spaced intervals to a peptide backbone, serve as lubricants and protective agents. The body fluids of vertebrates are rich in glycoproteins secreted from various glands and organs. Constituents of blood plasma which are glycoproteins include the transport proteins transferrin, ceruloplasmin, and transcobalamin I as well as the immunoglobulins, all the known clotting factors, and many of the components of complement. Follicle-stimulating hormone, luteinizing hormone, and thyroid-stimulating hormone (secreted by the pituitary) and chorionic gonadotropin are all glycoproteins as are the enzymes ribonuclease and deoxyribonuclease (secreted by the pancreas) and α-amylase (secreted by the salivary glands). Fungi secrete a number of glycoprotein enzymes, for example, Taka-amylase and invertase. Another group of glycoproteins are those which occur as integral components of cell membranes in a variety of species. Enveloped viruses contain surface glycoproteins that are involved in the attachment of the virus to its host, and in eukaryotic cells the histocompatibility antigens are membrane glycoproteins. There is a growing body of evidence to suggest that cell surface glycoproteins are involved in a number of physiologically important functions such as cell-cell interaction, adhesion of cells to substratum, and migration of cells to particular organs, for example, the “homing” of lymphocytes to the spleen and the metastasis of tumor cells to preferred sites.

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References

  • Allen, A. K., and Neuberger, A., 1973, Purification and properties of the lectin from potato tubers, a hydroxyproline-containing glycoprotein, Biochem. J. 135:307.

    PubMed  CAS  Google Scholar 

  • Allen, A. K., Desai, N. N., and Neuberger, A., 1976, The structure of a glycopeptide isolated from potato lectin, Abstracts of the 10th Int. Congress of Biochem., Hamburg, p. 503.

    Google Scholar 

  • Arima, T., and Spiro, R. G., 1972, Studies of the carbohydrate units of thyroglobulin, J. Biol. Chem. 247:1836.

    PubMed  CAS  Google Scholar 

  • Baenziger, J. U., 1975, Determination of the complete sequence of the oligosaccharide units present on IgG, IgE, and IgA1 myeloma proteins, Ph.D. thesis, Washington University, St. Louis, Mo., 136 pp.

    Google Scholar 

  • Baenziger, J. U., and Fiete, D., 1979, Structure of the complex oligosaccharides of fetuin, J. Biol. Chem. 254:789.

    PubMed  CAS  Google Scholar 

  • Baenziger, J., and Kornfeld, S., 1974a, Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation, and structure of the asparagine-linked oligosaccharide units, J. Biol. Chem. 249:7260.

    PubMed  CAS  Google Scholar 

  • Baenziger, J., and Kornfeld, S., 1974b, Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units, J. Biol. Chem. 249:7270.

    PubMed  CAS  Google Scholar 

  • Baenziger, J., Kornfeld, S., and Kochwa, S., 1974, Structure of the carbohydrate units of IgE immunoglobulin. II. Sequence of the sialic acid-containing glycopeptides. J. Biol. Chem. 249:1897.

    PubMed  CAS  Google Scholar 

  • Bahl, O. P., 1969, Human chorionic gonadotropin. II Nature of the carbohydrate units, J. Biol. Chem. 244:575.

    PubMed  CAS  Google Scholar 

  • Bahl, O. P., Carlson, R. B., Bellisario, R., and Swaminathan, N., 1972, Human chorionic gonadotropin: Amino acid sequence of the α and β subunits, Biochem. Biophys. Res. Commun. 48:416.

    Article  PubMed  CAS  Google Scholar 

  • Baig, M. M., and Aminoff, D., 1972, Glycoproteins and blood group activity. I. Oligosaccharides of serologically inactive hog submaxillary glycoproteins, J. Biol. Chem. 247:6111.

    PubMed  CAS  Google Scholar 

  • Bertolini, M., and Pigman, W., 1970, The existence of oligosaccharides in bovine and ovine submaxillary mucins, Carbohydr. Res. 14:53.

    Article  CAS  Google Scholar 

  • Bhattacharyya, S. N., and Lynn, W. S. 1977, Structural studies on the oligosaccharides of a glycoprotein isolated from alveoli of patients with alveolar proteinosis, J. Biol. Chem. 252:1172.

    PubMed  CAS  Google Scholar 

  • Bhavanandan, V. P., Umemoto, J., Banks, J. R., and Davidson, E. A., 1977, Isolation and partial characterization of sialoglycopeptides produced by a murine melanoma, Biochemistry 16:4426.

    Article  PubMed  CAS  Google Scholar 

  • Björndal, H., Lindberg, B., and Svensson, S., 1967a, Gas-liquid chromatography of partially methylated alditols as their acetates, Acta Chem. Scand. 21:1801.

    Article  Google Scholar 

  • Björndal, H., Lindberg, B., and Svensson, S., 1967b, Mass spectrometry of partially methylated alditol acetates, Carbohydr. Res. 5:433.

    Article  Google Scholar 

  • Björndal, H., Hellerqvist, C. G., Lindberg, B., and Svensson, S., 1970, Gas-liquid chromatography and mass spectrometry in methylation analysis of polysaccharides, Angew. Chem. Int. Ed. Engl. 9:610.

    Article  Google Scholar 

  • Bray, B. A., Lieberman, R., and Meyer, K., 1967, Structure of human skeletal keratosulfate: The linkage region, J. Biol. Chem. 242:3373.

    PubMed  CAS  Google Scholar 

  • Butler, W. T., and Cunningham, L. W., 1966, Evidence for the linkage of a disaccharide to hydroxylsine in tropocollagen, J. Biol. Chem. 241:3882.

    PubMed  CAS  Google Scholar 

  • Carlson, D. M., 1968, Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins, J. Biol. Chem. 243:616.

    PubMed  CAS  Google Scholar 

  • Chapman, A., and Kornfeld, R., 1979, Structure of the high mannose oligosaccharides of a human IgM myeloma protein, J. Biol. Chem. 254:816.

    PubMed  CAS  Google Scholar 

  • Codington, J. F., Linsley, K. B., Jeanloz, R. W., Irimura, T., and Osawa, T., 1975, Immunochemical and chemical investigations of the structure of glycoprotein fragments obtained from epiglycanin, a glycoprotein at the surface of the TA-3Ha cancer cell, Carbohydr. Res. 40:171.

    Article  PubMed  CAS  Google Scholar 

  • DeVries, A. L., Vandenheede, J., and Feeney, R. E., 1971, Primary structure of freezing-point-depressing glycoproteins, J. Biol. Chem. 246:305.

    PubMed  CAS  Google Scholar 

  • Endo, Y., Yamashita, K., Han, Y. N., Iwanaga, S., and Kobata, A. 1977, The carbohy drate structure of a glycopeptide released by action of plasma kallikrein on bovine plasma high-molecular-weight kininogen, J. Biochem. Tokyo 82:545.

    PubMed  CAS  Google Scholar 

  • Feizi, T., Kabat, E. A., Vicari, G., Anderson, B., and Marsh, W. L., 1971, Immunochemical studies on blood groups, J. Immunol. 106:1578.

    PubMed  CAS  Google Scholar 

  • Finne, J., 1975, Structure of the O-glycosidically linked carbohydrate units of rat brain glycoproteins, Biochim. Biophys. Acta 412:317.

    PubMed  CAS  Google Scholar 

  • Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K., 1978, Determination of the primary structures of 16 asialo-carbohydrate units derived from human plasma α1acid glycoprotein by 360-MHz 1H NMR spectroscopy and permethylation analysis, Biochemistry 17:5206.

    Article  PubMed  CAS  Google Scholar 

  • Frangione, B., and Wolfenstein-Todel, C., 1972, Partial duplication in the “hinge” region of IgA1 myeloma proteins, Proc. Natl. Acad. Sci. U.S.A. 69:3673.

    Article  PubMed  CAS  Google Scholar 

  • Fukuda, M., Kondo, T., and Osawa, T., 1976, Studies on the hydrazinolysis of glycoproteins, core structures of oligosaccharides obtained from porcine thyroglobulin and pineapple stem bromelain, J. Biochem. Tokyo 80:1223.

    PubMed  CAS  Google Scholar 

  • Fukuda, M., Papermaster, D., and Hargrave, P. A., 1979, Rhodopsin carbohydrate: Structure of small oligosaccharides attached at two sites near the amino-terminus, J. Biol. Chem. 254:8201.

    PubMed  CAS  Google Scholar 

  • Gibson, R., Schlesinger, S., and Kornfeld, S., 1979, The nonglycosylated glycoprotein of VSV is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures, J. Biol. Chem. 254:3600.

    PubMed  CAS  Google Scholar 

  • Gottschalk, A. (ed.), 1972, Glycoproteins, 2nd ed., Elsevier, Amsterdam.

    Google Scholar 

  • Glockner, W. M., Newman, R. A., Dahr, W., and Uhlenbruck, G., 1976, Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes, Biochim. Biophys. Acta 443:402.

    Article  PubMed  CAS  Google Scholar 

  • Hakomori, S., 1964, A rapid permethylation of glycolipid, and polysaccharide catalyzed by methylsulfinyl carbanion in dimethyl sulfoxide, J. Biochem. Tokyo 55:205.

    PubMed  CAS  Google Scholar 

  • Hallgren, P., Lundblad, A., and Svensson, S., 1975, A new type of carbohydrate protein linkage in a glycopeptide from normal human urine, J. Biol. Chem. 250:5312.

    PubMed  CAS  Google Scholar 

  • Hara, K., Ruthnam, P., and Saxena, B., 1978, Structure of the carbohydrate moieties of α subunits of human follitropin, lutropin and thyrotropin, J. Biol. Chem. 253:1582.

    PubMed  CAS  Google Scholar 

  • Heath, M. F., and Northcote, D. H., 1971, Glycoprotein of the wall of sycamore tissue-culture cells, Biochem. J. 125:952.

    Google Scholar 

  • Hickman, S., Kornfeld, R., Osterland, C. K., and Kornfeld S., 1972, The structure of the glycopeptides of a human γM-immunoglobulin, J. Biol. Chem. 247:2156.

    PubMed  CAS  Google Scholar 

  • Higashi, H., Naiki, M., Matuo, S., and Okouchi K., 1977, Antigen of “serum sickness” type of antibodies in human sera: Identification as gangliosides with N-glycolyl-neuraminic acid, Biochem. Biophys. Res. Commun. 79:388.

    Article  PubMed  CAS  Google Scholar 

  • Hirs, C. H. W., Moore, S., and Stein, W. H., 1960, The sequence of the amino acid residues in performic acid-oxidized ribonuclease, J. Biol. Chem. 235:633.

    PubMed  CAS  Google Scholar 

  • Huang, C. C., Mayer, H. E., Jr., and Montgomery, R., 1970, Microheterogeneity and paucidispersity of glycoproteins. Part I. The carbohydrates of chicken ovalbumin, Carbohydr. Res. 13:127.

    Article  CAS  Google Scholar 

  • Hubbard, S. C., and Robbins, P. W., 1979, Synthesis and processing of protein-linked oligosaccharides in vivo, J. Biol. Chem. 254:4568.

    PubMed  CAS  Google Scholar 

  • Hughes, R. C., 1973, Glycoproteins as components of cellular membranes, Prog. Biophys. Mol. Biol. 26:189.

    Article  PubMed  CAS  Google Scholar 

  • Hunt, L. A., Etchison, J. R., and Summers, D. F., 1978, Oligosaccharide chains are trimmed during synthesis of the envelope glycoprotein of vesicular stomatitis virus, Proc. Natl. Acad. Sci. U.S.A. 75:754.

    Article  PubMed  CAS  Google Scholar 

  • Isemura, M., Ikenaka, T., and Matsushima, Y., 1973, Comparative study of carbohydrate-protein complexes. I. The structures of glycopeptides derived from cuttlefish skin collagen, J. Biochem. Tokyo 74:11.

    PubMed  CAS  Google Scholar 

  • Ito, S., Muramatsu, T., and Kobata, A., 1975, Release of galactosyl oligosaccharides by endo-β-N-acetylglucosaminidase D, Biochem. Biophys. Res. Commun. 63:938.

    Article  PubMed  CAS  Google Scholar 

  • Ito, S., Yamashita, K., Spiro, R. G., and Kobata, A., 1977, Structure of a carbohydrate moiety of a unit A glycopeptide of calf thyroglobulin, J. Biochem. Tokyo 81:1621.

    PubMed  CAS  Google Scholar 

  • Jackson, R. L., and Hirs, C. H. W., 1970a, The primary structure of porcine pancreatic ribonuclease. II. The amino acid sequence of the reduced S-aminoethylated protein, J. Biol. Chem. 245:637.

    PubMed  CAS  Google Scholar 

  • Jackson, R. L., and Hirs, C. H. W., 1970b, The primary structure of porcine pancreatic ribonuclease. I. The distribution and sites of carbohydrate attachment, J. Biol. Chem. 245:624.

    PubMed  CAS  Google Scholar 

  • Kawasaki, T., and Ashwell, G., 1976, Carbohydrate structure of glycopeptides isolated from an hepatic membrane-binding protein specific for asialoglycoproteins, J. Biol. Chem. 251:5292.

    PubMed  CAS  Google Scholar 

  • Kieras, F. J., 1974, The linkage region of cartilage keratan sulfate, J. Biol. Chem. 249:7506.

    PubMed  CAS  Google Scholar 

  • Koide, N., and Muramatsu, T., 1974, Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins: Purification and properties of the enzyme from Diplococcus pneumoniae, J. Biol. Chem. 249:4897.

    PubMed  CAS  Google Scholar 

  • Koide, N., Nose, M., and Muramatsu, T., 1977, Recognition of IgG by Fc receptor and complement: Effects of glycosidase digestion, Biochem. Biophys. Res. Commun. 75:838.

    Article  PubMed  CAS  Google Scholar 

  • Kondo, T., Fukuda, M., and Osawa, T., 1977, The structure of unit B-type glycopeptides from porcine thyroglobulin, Carbohydr. Res. 58:405.

    Article  PubMed  CAS  Google Scholar 

  • Kornfeld, R., 1978, Structure of the oligosaccharides of three glycopeptides from calf thymocyte plasma membranes, Biochemistry 17:1415.

    Article  PubMed  CAS  Google Scholar 

  • Kornfeld, R., and Kornfeld, S., 1970, The structure of phytohemagglutinin receptor site from human erythrocytes, J. Biol. Chem. 245:2536.

    PubMed  CAS  Google Scholar 

  • Kornfeld, R., and Kornfeld, S., 1976, Comparative aspects of glycoprotein structure. Annu. Rev. Biochem. 45:217.

    Article  PubMed  CAS  Google Scholar 

  • Kornfeld, R., Keller, J., Baenziger, J., and Kornfeld, S., 1971, The structure of the glycopeptide of human γG myeloma proteins, J. Biol. Chem. 246:3259.

    PubMed  CAS  Google Scholar 

  • Kornfeld, S., and Kornfeld, R., 1971, The structure of phytohemagglutinin receptor sites, in: Glycoproteins of Blood Cells and Plasma (G. A. Jamieson and T. J. Greenwalt, eds.), pp. 50–68, Lippincott, Philadelphia.

    Google Scholar 

  • Kornfeld, S., Li, E., and Tabas, I., 1978, Characterization of the processing intermediates in the synthesis of the complex oligosaccharide unit of the vesicular stomatitis virus G protein, J. Biol. Chem. 253:7771.

    PubMed  CAS  Google Scholar 

  • Krusius, T., Finne, J., and Rauvala, H., 1976, The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin A-Sepharose, FEBS Lett. 71:117.

    Article  CAS  Google Scholar 

  • Laine, R. A., Esselman, W. J., and Sweeley, C. C., 1972, Gas-liquid chromatography of carbohydrates, Methods Enzymol. 28B:159.

    Article  Google Scholar 

  • Lamport, D. T. A., 1969, The isolation and partial characterization of hydroxyproline-rich glycopeptides obtained by enzymic degradation of primary cell walls, Biochemistry 8:1155.

    Article  PubMed  CAS  Google Scholar 

  • Lamport, D. T. A., Katona, L., and Roerig, S., 1973, Galactosylserine in extensin, Biochem. J. 135:125.

    Google Scholar 

  • Larriba, G., Klinger, M. Sramek, S., and Steiner, S. 1977, Novel fucose-containing components from rat tissues, Biochem. Biophys. Res. Commun. 77:79.

    Article  PubMed  CAS  Google Scholar 

  • Leavitt, R., Schlesinger, S., and Kornfeld, S., 1977, Impaired intracellular migration and altered solubility of nonglycosylated glycoproteins of vesicular stomatitis virus and Sindbis virus, J. Biol. Chem. 252:9018.

    PubMed  CAS  Google Scholar 

  • Lee, Y. C., 1972, Analysis of sugars by automated liquid chromatography, Methods Enzymol. 28B:63.

    Article  Google Scholar 

  • Lee, Y. C., and Scocca, J. R., 1972, A common structural unit in asparagine-oligosaccharides of several glycoproteins from different sources, J. Biol. Chem. 247:5753.

    PubMed  CAS  Google Scholar 

  • Li, E., and Kornfeld, S., 1979, Structural studies of the major high mannose oligosaccharide units from Chinese hamster ovary cell glycoproteins, J. Biol. Chem. 254:1600.

    PubMed  CAS  Google Scholar 

  • Li, E., Tabas, I., and Kornfeld, S., 1978, Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein, J. Biol. Chem. 253:7762.

    PubMed  CAS  Google Scholar 

  • Li, Y. T., and Lee, Y. C., 1972, Pineapple α-and β-D-mannopyranosidases and their action on core glycopeptides, J. Biol. Chem. 247:3677.

    PubMed  CAS  Google Scholar 

  • Liang, C.-J., Yamashita, K., Muellenberg, C. G., Shichi, H., and Kobata, A., 1979, Structure of the carbohydrate moieties of bovine rhodopsin, J. Biol. Chem. 254:6414.

    PubMed  CAS  Google Scholar 

  • Lombart, C. G., and Winzler, R. J., 1974, Isolation and characterization of oligosaccharides from canine submaxillary mucin, Eur. J. Biochem. 49:77.

    Article  PubMed  CAS  Google Scholar 

  • Mahieu, P. M., Lambert, P. H., and Maghuin-Rogister, G. R., 1973, Primary structure of a small glycopeptide isolated from human glomerular basement membrane and carrying a major antigenic site, Eur. J. Biochem. 40:599.

    Article  PubMed  CAS  Google Scholar 

  • Marks, G. S., Marshall, R. D., and Neuberger, A., 1963, Carbohydrates in protein. 6. Studies on the carbohydrate-peptide bond in hen’s egg albumin, Biochem. J. 87:274.

    PubMed  CAS  Google Scholar 

  • Marshall, R. D., 1972, Glycoproteins, Annu. Rev. Biochem. 41:673.

    Article  PubMed  CAS  Google Scholar 

  • Marshall, R. D., and Neuberger, A., 1964, Carbohydrates in protein. VIII. The isolation of 2-acetamide-l-(l-β-aspartamido)-1,2-dideoxy-β-D-glucose from hen’s egg albumin, Biochemistry 3:1596.

    Article  PubMed  CAS  Google Scholar 

  • Michalski, J. C., Strecker, G., Fournet, B., Cantz, M., and Spranger, J., 1977, Structures of sialyl-oligosaccharides excreted in the urine of a patient with mucolipidosis I, FEBS Lett. 79:101.

    Article  PubMed  CAS  Google Scholar 

  • Misaki, A., and Goldstein, I. J., 1977, Glycosyl moiety of the lima bean lectin, J. Biol. Chem. 252:6995.

    PubMed  CAS  Google Scholar 

  • Mizuochi, T., Yamashita, K., Fujikawa, K., Kisiel, W., and Kobata, A., 1979, The carbohydrate of bovine prothrombin, J. Biol. Chem. 254:6419.

    PubMed  CAS  Google Scholar 

  • Montreuil, J., 1975, Recent data on the structure of the carbohydrate moiety of glycoproteins—Metabolic and biologic implications, Pure Appl. Chem. 42:431.

    Article  CAS  Google Scholar 

  • Morell, A. G., and Ashwell, G., 1972, Tritium labeling of glycoproteins that contain terminal galactose residues, Methods Enzymol. 28B:205.

    Article  Google Scholar 

  • Morgan, P. H., Jacobs, H. G., Segrest, J. P. and Cunningham, L. W., 1970, A comparative study of glycoptroteins derived from selected vertebrate collagens, J. Biol. Chem. 245:5042.

    PubMed  CAS  Google Scholar 

  • Muir, L., and Lee, Y. C., 1969, Structures of the D-galactose oligosaccharides from earthworm cuticle collagen, J. Biol. Chem. 244:2343.

    PubMed  CAS  Google Scholar 

  • Muir, L, and Lee, Y. C., 1970, Glycopeptides from earthworm cuticle collagen, J. Biol. Chem. 245:502.

    PubMed  CAS  Google Scholar 

  • Nakajima, T., and Ballou, C.E., 1974a, Characterization of the carbohydrate fragments obtained from Saccharomyces cerevisiaemannan by alkaline degradation, J. Biol. Chem. 249:7679.

    PubMed  CAS  Google Scholar 

  • Nakajima, T., and Ballou, C. E., 1974b, Structure of the linkage region between the polysaccharide and protein parts of Saccharomyces cerevisiaemannan, J. Biol. Chem. 249:7685.

    PubMed  CAS  Google Scholar 

  • Newman, R. A., Glockner, W. M., and Uhlenbruck, G., 1976, Immunochemical detection of the Thomsen-Friedenreich antigen (T-antigen) on the pig lymphocyte plasma membrane, Eur. J. Biochem. 64:373.

    Article  PubMed  CAS  Google Scholar 

  • Ng Ying Kin, N. M. K., and Wolfe, L. S., 1974, Oligosaccharides accumulating in the liver from a patient with GM2-gangliosidosis variant O (Sandhoff-Jatzkewitz disease), Biochem. Biophys. Res. Commun. 59:837.

    Article  PubMed  CAS  Google Scholar 

  • Nishigaki, M., Yamashita, K., Matsuda, I., Arashima, S., and Kobata, A., 1978, Urinary oligosaccharides of fucosidosis, J. Biochem. Tokyo 84:823.

    PubMed  CAS  Google Scholar 

  • Oates, M. D., Rosbottom, A. C., and Schrager, J., 1974, Further investigations into the structure of human gastric mucin: The structural configuration of the oligosaccharide chains, Carbohydr. Res. 34:115.

    Article  PubMed  CAS  Google Scholar 

  • Ogata, S., Muramatsu, T., and Kobata, A., 1975, Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose, J. Biochem. Tokyo 78:687.

    PubMed  CAS  Google Scholar 

  • Pazur, J. H., Knull, H. R., and Cepure, A., 1971, Glycoenzymes: Structure and properties of the two forms of glucoamylase from Aspergillus niger, Carbohydr. Res. 20:83.

    Article  PubMed  CAS  Google Scholar 

  • Plummer, T. H., Jr., 1968, Glycoproteins of bovine pancreatic juice, J. Biol. Chem. 243:5961.

    PubMed  CAS  Google Scholar 

  • Plummer, T. H., Jr., and Hirs, C. H. W., 1964, On the structure of bovine pancreatic ribonuclease B: Isolation of a glycopeptide, J. Biol. Chem. 239:2530.

    PubMed  CAS  Google Scholar 

  • Puett, D., 1973, Conformational studies on a glycosylated bovine pancreatic ribonuclease, J. Biol. Chem. 248:3566.

    PubMed  CAS  Google Scholar 

  • Purkayastha, S., Rao, C. V. N., and Lamm, M. E., 1979, Structure of the carbohydrate chain of free secretory component from human milk, J. Biol. Chem. 254:6583.

    PubMed  CAS  Google Scholar 

  • Raizada, M. K., Schutzbach, J. S., and Ankel, H., 1975, Cryptococcus laurentiicell envelope glycoprotein, J. Biol. Chem. 250:3310.

    PubMed  CAS  Google Scholar 

  • Reading, C. L., Penhoet, E. E., and Ballou, C. E., 1978, Carbohydrate structure of vesicular stomatitis virus glycoprotein, J. Biol. Chem. 253:5600.

    PubMed  CAS  Google Scholar 

  • Richards, F. M., and Wyckoff, H. W., 1971, Bovine pancreatic ribonuclease, in: The Enzymes (P. D. Boyer, ed.), 3rd ed., Vol. 4, pp. 647–806, Academic Press, New York.

    Google Scholar 

  • Robbins, P. W., Hubbard, S. C., Turco, S. J., and Wirth, D. F., 1977, Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins, Cell 11:893.

    Article  Google Scholar 

  • Robertson, M. A., Etchison, J. R., Robertson, J. S., Summers, D. F., and Stanley, P., 1978, Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells, Cell 13:515.

    Article  PubMed  CAS  Google Scholar 

  • Rosenthal, A. L., and Nordin, J. H., 1975, Enzymes that hydrolyze fungal cell wall polysaccharides, J. Biol. Chem. 250:5295.

    PubMed  CAS  Google Scholar 

  • Schwarz, R. T., Rohrschneider, J. M., and Schmidt, M. F. G., 1976, Suppression of glycoprotein formation of semliki forest, influenza, and avian sarcoma virus by tunicamycin, J. Virol. 19:782.

    PubMed  CAS  Google Scholar 

  • Schwarzmann, G., Hatcher, V. B., and Jeanloz, R. W., 1978, Purification and structural elucidation of several carbohydrate side chains from α1acid glycoprotein, J. Biol. Chem. 253:6983.

    PubMed  CAS  Google Scholar 

  • Sentandreu, R., and Northcote, D. H., 1969, The characterization of oligosaccharides attached to threonine and serine in a mannan glycopeptide obtained from the cell wall of yeast, Carbohydr. Res. 10:584.

    Article  CAS  Google Scholar 

  • Shier, W. T., Lin, Y., and De Vries, A. L., 1975, Structure of the carbohydrate of antifreeze glycoproteins from an Antarctic fish, FEBS Lett. 54:135.

    Article  PubMed  CAS  Google Scholar 

  • Shimizu, A., Putnam, F. W., Paul, C., Clamp, J. R., and Johnson, I., 1971, Structure and role of the five glycopeptides of human IgM immunoglobulins, Nature (London), New Biol. 231:73.

    CAS  Google Scholar 

  • Silverton, E. W., Manuel, A. N., and Davies, D. R., 1977, Three-dimensional structure of an intact human immunoglobulin, Proc. Natl. Acad. Sci. U.S.A. 74:5740.

    Article  Google Scholar 

  • Spik, G., Bayard, B., Fournet, B., Strecker, G., Bouquelet, S., and Montreuil, J., 1975, Complete structure of the two carbohydrate units of human serotransferrin, FEBS Lett. 50:296.

    PubMed  CAS  Google Scholar 

  • Spinola, M., and Jeanloz, R. W., 1970, The synthesis of a di-N-acetylchitobiose asparagine derivative, 2-acetamido-4-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-l-N-(4-L-aspartyl-2-deoxy-β-D-glucopyranosylamine, J. Biol. Chem. 245:4158.

    PubMed  CAS  Google Scholar 

  • Spiro, R. G., 1966, Characterization of carbohydrate units of glycoproteins, Methods Enzymol. 8:26.

    Article  CAS  Google Scholar 

  • Spiro, R. G., 1967, The structure of the disaccharide unit of the renal glomerular basement membrane, J. Biol. Chem. 242:4813.

    PubMed  CAS  Google Scholar 

  • Spiro, R. G. 1973, Glycoproteins, Adv. Protein Chem. 27:349.

    Article  PubMed  CAS  Google Scholar 

  • Spiro, R. G., and Bhoyroo, V. D., 1971, The carbohydrate of invertebrate collagens: A glucuronic acid-mannose disaccharide unit, Fed. Proc. 30:1223.

    Google Scholar 

  • Spiro, R. G., and Bhoyroo, V. D., 1974, Structure of the O-glycosidically linked carbohydrate units of fetuin, J. Biol Chem. 249:5704.

    PubMed  CAS  Google Scholar 

  • Strecker, G., Fournet, B., Spik, G., Montreuil, J., Durand, P., and Tondeur, M., 1977, Structure of 9 oligosaccharides and glycopeptides rich in fucose excreted in the urine of two patients with fucosidosis, C. R. Acad. Sci. (Paris) 284D:85.

    Google Scholar 

  • Sugahara, K., Okumura, T., and Yamashina, I., 1972, Purification of β-mannosidase from a snail, Achatina fulica, and its action on glycopeptides, Biochim. Biophys. Acta 268:488.

    PubMed  CAS  Google Scholar 

  • Sugahara, K., Funakoshi, S., Funakoshi, I., Aula, P., and Yamashina, I., 1976, Characterization of one neutral and two acidic glycoasparagines isolated from the urine of patients with asparatyl-glycosylaminuria, J. Biochem. Tokyo 80:195.

    PubMed  CAS  Google Scholar 

  • Sukeno, T., Tarentino, A. L., Plummer, T. H., Jr., and Maley, F., 1971, On the nature of α-mannosidase-resistant linkages in glycoproteins, Biochem. Biophys. Res. Commun. 45:219.

    Article  PubMed  CAS  Google Scholar 

  • Sukeno, T., Tarentino, A. L., Plummer, T. H., Jr., and Maley, F., 1972, Purification and properties of α-Dand β-D-mannosidases from hen oviduct, Biochemistry 11:1493.

    Article  PubMed  CAS  Google Scholar 

  • Tabas, I., and Kornfeld, S., 1978, Identification of an α-D-mannosidase activity involved in a late stage of processing of complex-type oligosaccharides, J. Biol. Chem. 253:7779.

    PubMed  CAS  Google Scholar 

  • Tabas, I., Schlesinger, S., and Kornfeld, S., 1978, The processing of high mannose oligosaccharides to form complex type oligosaccharides in the newly synthesized polypep-tides of the vesicular stomatitis virus G protein and the IgG heavy chain, J. Biol. Chem. 253:716.

    PubMed  CAS  Google Scholar 

  • Tai, T., Ito, S., Yamashita, K., Muramatsu, T., and Kobata, A., 1975a, Asparagine-linked oligosaccharide chains of IgG: A revised structure, Biochem. Biophys. Res. Commun. 65:968.

    Article  PubMed  CAS  Google Scholar 

  • Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y., and Kobata, A., 1975b, Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity, J. Biol. Chem. 250:8569.

    PubMed  CAS  Google Scholar 

  • Tai, T., Yamashita, K., Ito, S., and Kobata, A., 1977a, Structures of the carbohydrate moiety of ovalbumin glycopeptide III and the difference in specificity of endo-β-N-acetylglucosaminidases CII and H, J. Biol. Chem. 252:6687.

    PubMed  CAS  Google Scholar 

  • Tai, T., Yamashita, K., and Kobata, A., 1977b, The substrate specificities of endo-β-N-acetylglucosaminidases CII and H, Biochem. Biophys. Res. Commun. 78:434.

    Article  PubMed  CAS  Google Scholar 

  • Tarentino, A. L., and Maley, F. 1974, Purification and properties of an endo-β-N-acetyl-glucosaminidase from Streptomyces griseus, J. Biol. Chem. 249:811.

    PubMed  CAS  Google Scholar 

  • Tarentino, A. L., and Maley, F., 1976, Purification and properties of an endo-β-N-acetyl-glucosaminidase from hen oviduct, J. Biol. Chem. 251:6537.

    PubMed  CAS  Google Scholar 

  • Tarentino, A., Plummer, T. H., Jr., and Maley, F., 1970, Studies on the oligosaccharide sequence of ribonuclease B, J. Biol. Chem. 245:4150.

    PubMed  CAS  Google Scholar 

  • Tarentino, A. L., Plummer, T. H., and Maley, F., 1974, The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H, J. Biol. Chem. 249:818.

    PubMed  CAS  Google Scholar 

  • Thomas, D. B., and Winzler, R. J., 1969, Structural studies on human erythrocyte glycoproteins: Alkali-labile oligosaccharides, J. Biol. Chem. 244:5943.

    PubMed  CAS  Google Scholar 

  • Thomas, D. B., and Winzler, R. J., 1971, Structure of glycoproteins of human erythrocytes: Alkali-stable oligosaccharides, Biochem. J. 124:55.

    PubMed  CAS  Google Scholar 

  • Toyoshima, S., Fukuda, M., and Osawa, T., 1972, Chemical nature of the receptor site for various phytomitogens, Biochemistry 11:4000.

    Article  PubMed  CAS  Google Scholar 

  • Toyoshima, S., Fukuda, M., and Osawa, T., 1973, The presence of β-mannosidic linkage in acidic glycopeptide from porcine thyroglobulin, Biochem. Biophys. Res. Commun. 51:945.

    Article  PubMed  CAS  Google Scholar 

  • Tsay, G. C., Dawson, G., and Sung, S.-S. J., 1975, Structure of the accumulating oligosaccharide in fucosidosis, J. Biol. Chem. 251:5852.

    Google Scholar 

  • Van Lenten, L., and Ashwell, G., 1972, Tritium-labeling of glycoproteins that contain sialic acid, Methods Enzymol. 28B:209.

    Article  Google Scholar 

  • Wang, C. F. F., and Hirs, C. H. W., 1977, Influence of the heterosaccharides in porcine pancreatic ribonuclease on the conformation and stability of the protein, J. Biol. Chem. 252:8358.

    PubMed  CAS  Google Scholar 

  • Watkins, W. M., 1972, Blood-group specific substances, in: Glycoproteins(A. Gottschalk, ed.), 2nd ed., Part B, p. 830, Elsevier, Amsterdam.

    Google Scholar 

  • Wolfe, L. S., Senior, R. G., and Ng Ying Kin, N. M. K., 1974, The structures of oligosaccharides accumulating in the liver of GM1-gangliosidosis, type I, J. Biol. Chem. 249:1828.

    PubMed  CAS  Google Scholar 

  • Yamaguchi, H., Ikenaka, T., and Matsushima, Y., 1971, The complete sequence of a glycopeptide obtained from Taka-amylase A, J. Biochem. Tokyo 70:587.

    PubMed  CAS  Google Scholar 

  • Yamashita, K., Tachibana, Y., and Kobata, A., 1978, The structures of the galactose-containing sugar chains of ovalbumin, J. Biol. Chem. 253:3862.

    PubMed  CAS  Google Scholar 

  • Yasuda, Y., Takahashi, N., and Murachi, T., 1970, The composition and structure of carbohydrate moiety of stem bromelain, Biochemistry 9:25.

    Article  PubMed  CAS  Google Scholar 

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Kornfeld, R., Kornfeld, S. (1980). Structure of Glycoproteins and Their Oligosaccharide Units. In: Lennarz, W.J. (eds) The Biochemistry of Glycoproteins and Proteoglycans. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1006-8_1

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  • DOI: https://doi.org/10.1007/978-1-4684-1006-8_1

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