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Circulating Sialyl Compounds

  • Chapter
Biological Roles of Sialic Acid

Abstract

A number of biologically active glycoproteins found in mammalian plasma contain sialic acid. The role(s) of sialic acid on circulating sialoglycoproteins has received much attention during the past 10–15 years. Areas of particular interest are (1) circulating sialoglycoproteins in disease and (2) the function of sialic acid in determining survival time of circulating sialoglycoproteins. Changes in the levels of plasma sialoglycoproteins have been reported in a variety of diseases (for review, Spiro, 1970; Winzler, 1971). Changes in sialic acid content of specific circulating sialoglycoproteins affect their rate of clearance from plasma (for review, Ashwell and Morell, 1975). Enzymatic, hormonal, and immunogenic activities of various sialoglycoproteins have been found to be related in some degree to their sialic acid content. This chapter will not attempt to review all the work that has been done on circulating sialoglycoproteins, but will restrict itself to aspects of the following: (a) a survey of circulating sialoglycoproteins, (b) changes in plasma sialic acid levels in disease, and (c) possible biological roles for sialic acid. Synthesis and catabolism of sialic-acid-containing compounds are reviewed in Chapters 4 and 5, respectively.

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References

  • Agishev, V. G., 1970, Concerning the changes of the proteins in the blood serum in some infectious psychoses, Psikhiar. S. S. Korsakova 70: 1343–1348.

    CAS  Google Scholar 

  • Anderson, A. J., 1965, Factors affecting the amount and composition of the serum seromucoid fraction, Nature 208: 491–492.

    PubMed  CAS  Google Scholar 

  • Arfors, K. E., Beckman, L., and Lundin, L. G., 1963, Further studies on the association between human serum phosphatases and blood groups, Acta Genet. Statist. 13: 366–368.

    CAS  Google Scholar 

  • Ashwell, G., and Morell, A. G., 1975, The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins, Adv. Enzymol. 41: 99–128.

    Google Scholar 

  • Athineos, E., Thornton, M., and Winzler, R. J., 1962, Comparative antigenicity of native and “desialized” orosomucoid in rabbits, Proc. Soc. Exp. Biol. Med. 111: 353–356.

    PubMed  CAS  Google Scholar 

  • Augustinsson, K.-B., and Ekedahl, G., 1962, The properties of neuraminidase-treated serum cholinesterase, Biochim. Biophys. Acta 56: 392–393.

    PubMed  CAS  Google Scholar 

  • Baker, E., Shaw, D. C., and Morgan, E. H., 1968, Isolation and characterization of rabbit serum and milk transferrins. Evidence for difference in sialic acid content only, Biochemistry 7: 1371–1378.

    PubMed  CAS  Google Scholar 

  • Bates, R. W., and Warren, L., 1963, Studies on the sialic acid content of thyroid glands, Endocrinology 73: 1–4.

    PubMed  CAS  Google Scholar 

  • Barr, W. A., and Collee, J. G., 1967, Differences in the biological and immunological activities of human chorionic gonadotiopin after removal of sialic acid by enzymic hydrolysis, J. Endocrinol. 38: 395–399.

    PubMed  CAS  Google Scholar 

  • Bell, O. F., and Carrell, R. W., 1973, Basis of the defect in α-1-antitrypsin deficiency, Nature 243: 410–411.

    PubMed  CAS  Google Scholar 

  • Blumberg, B. S., and Warren, L., 1961, The effect of sialidase on transferrins and other serum proteins, Biochim. Biophys. Acta 50: 90–101.

    CAS  Google Scholar 

  • Bocci, V., Viti, A., Russi, M., and Rita, G., 1971, Isoelectric fractionation of desialyzed interferon. Experientia 27: 1160–1161.

    PubMed  CAS  Google Scholar 

  • Bosmann, H. B., 1974, Red cell hydrolases. Vox Sang. 26: 497–512.

    PubMed  CAS  Google Scholar 

  • Braunstein, G. D., Reichert, Jr., L. E., Van Hall, E. V., Vaitukaitis, J. L., and Ross, G. T., 1971, The effects of desialylation on the biologic and immunologic activity of human pituitary luteinizing hormone, Biochem. Biophys. Res. Commun. 42: 962–967.

    PubMed  CAS  Google Scholar 

  • Cabezas, J. A., and Porto, E., 1970, Acidos Siálicos. XIII. Contenido en acido N-acetilneuramínico, hexosaminas y ácido pirúvico, y actividad N-acetil-β-glucosaminidásica de sueros normales y cancerosos, Rev. Esp. Fisiol. 26: 339–345.

    PubMed  CAS  Google Scholar 

  • Chakrabarti, T., Pawar, R. B., Shastri, M. G., Choudhary, D. R., Chakrabarti, C. H., and Dias, P. D., 1972, N-Acetyl neuraminic acid level in the erythrocyte membrane and serum of patients suffering from diabetes mellitus, Ind. J. Med. Res. 60: 1038–1042.

    CAS  Google Scholar 

  • Chandrasekhar, N., Warren, L., Osbahr, A. J., and Laki, K., 1962, Role of sialic acid in fibrinogen, Biochim. Biophys. Acta 63: 337–339.

    PubMed  CAS  Google Scholar 

  • Chandrasekhar, N., Osbahr, A. J., and Laki, K., 1966, Identification of sialic acids in human and bovine fibrinogen, Biochem. Biophys. Res. Commun. 23: 757–760.

    PubMed  CAS  Google Scholar 

  • Chen, S.-H., and Sutton, H. E., 1967, Bovine transferrins: Sialic acid and the complex phenotype, Genetics 56: 425–430.

    PubMed  CAS  Google Scholar 

  • Clamp, J. R., and Johnson, I., 1972, Immunoglobulins in: Glycoproteins, Part A (A. Gottschalk, ed.) p. 612–652, Elsevier Publishing Co., New York.

    Google Scholar 

  • Cowan, N. J., and Robinson, G. B., 1972, The sequence of addition of terminal sugars to an immunoglobulin a myeloma protein, Biochem. J. 126: 751–754.

    PubMed  CAS  Google Scholar 

  • Cuatrecases, P., and Illiano, G., 1971, Membrane sialic acid and the mechanism of insulin action in adipose tissue cells, J. Biol: Chem. 246: 4938–4946.

    Google Scholar 

  • Cunningham, L. W., 1971, Microheterogeneity and Function of Glycoproteins in Glycoproteins of Blood Cells and Plasma (G. A. Jamieson and T. J. Greenwalt, eds.), pp. 34–61, Lippincott Co., Philadelphia.

    Google Scholar 

  • Davis, M. M., and Richmond, J. E., 1968, Effect of dietary protein on serum proteins, Am. J. Physiol. 215: 366–369.

    PubMed  CAS  Google Scholar 

  • De Moor, P., Bouillon, R., and Van Mieghem, W., 1970, Transcortin activity as related to the age at discovery of diabetes mellitus, Clin. Chim. Acta 30: 627–633.

    PubMed  Google Scholar 

  • Engen, R. L., 1970, Effect of steroids on serum sialic acid values in the canine, Proc. Soc. Exp. Biol. Med. 135: 778–780.

    PubMed  CAS  Google Scholar 

  • Engen, R. L., 1971, Serum sialic acid values in dogs with canine distemper, Am. J. Vet. Res. 32: 803–804.

    PubMed  CAS  Google Scholar 

  • Finnegan, D. J., and Hope, R. M., 1970, The role of sialic acid in the serum amylase isoenzyme pattern of the marsupial mouse Sminthopsis crassicaudata, Austr. J. Exp. Biol. Med. Sci. 48: 237–240.

    CAS  Google Scholar 

  • Gattegno, L., Bladier, D., and Cornillot, P., 1974, The role of sialic acid in the determination of survival of rabbit erythrocytes in the circulation, Carbohydrate Res. 34: 361–369.

    CAS  Google Scholar 

  • Goldwasser, E., Kung, C. K.-H., and Eliason, J., 1974, On the mechanism of erythropoietin-induced differentiation. XIII. The role of sialic acid in erythropoietin action, J. Biol. Chem. 249: 4202–4206.

    PubMed  CAS  Google Scholar 

  • Got, R., Cheftel, R.-I., Font, J., and Moretti, J., 1967, Étude de L’ α1-macroglobuline du serum de lapin. III. Biochimie de la copule glucidique, Biochim. Biophys. Acta 136: 320–330.

    PubMed  CAS  Google Scholar 

  • Gottschalk, A., Whitten, W. K., and Graham, E. R. B., 1960, Inactivation of folliclestimulating hormone by enzymic release of sialic acid, Biochim. Biophys. Acta 38: 183–184.

    PubMed  CAS  Google Scholar 

  • Gregoriadis, G., Morell, A. G., Steinlieb, I., and Scheinberg, I. H., 1970, Catabolism of desialylated ceruloplasmin in the liver, J. Biol. Chem. 245: 5833–5837.

    PubMed  CAS  Google Scholar 

  • Green, W. A., and Kay, C. M., 1963, The influence of organic solvents and enzyme modification on the secondary structure of fetuin, J. Biol. Chem. 238: 3640–3644.

    PubMed  CAS  Google Scholar 

  • Heilbronn, E., 1962, Treatment of horse serum cholinesterase with sialidase, Acta Chem. Scand. 16: 516.

    CAS  Google Scholar 

  • Heyward, J. T., Coleman, M. T., and Dowdle, W. R., 1972, Influenza antihemagglutinin and antinuraminidase activity of IgG and IgM in reference chicken antisera, Proc. Soc. Exp. Biol. Med. 140: 1289–1293.

    PubMed  CAS  Google Scholar 

  • Howard, C. B., and Kelleher, P. C., 1971, Plasma fucose and sialic acid concentrations during oral glucose tolerance tests in normal and diabetic (mellitus) humans, Clin. Chim. Acta 31: 75–80.

    PubMed  CAS  Google Scholar 

  • Itoh, C., Hashimoto, I., Onuma, Y., and Ishitoya, Y., 1968, Inhibitory effects of monoclonal immunoglobulins on anti-globulin reaction, Tohoku J. Exp. Med. 94: 307–313.

    CAS  Google Scholar 

  • Jakab, J. F., and Takács, L., 1970, Effect of liver injury and of induced inflammation on the serum glycoprotein level, Acta Med. Acad. Sci. Hung. 27: 57–63.

    PubMed  Google Scholar 

  • Jamieson, G. A., 1963, Carbohydrate chains of human transferrin, Fed. Proc. 22: 538.

    Google Scholar 

  • Jamieson, G. A., 1965, Studies on glycoproteins. 1. The carbohydrate portion of human ceruloplasmin, J. Biol. Chem. 240: 2019–2027.

    PubMed  CAS  Google Scholar 

  • Jamieson, G. A., 1971, in: Glycoproteins of Blood Cells and Plasma (G. A. Jamieson and T. J. Greenwalt, eds.), p. 68, Lippincott Co., Philadelphia.

    Google Scholar 

  • Jamieson, G. A., 1972, Ceruloplasmin, in Glycoproteins, Part A (A. Gottschalk, ed.), Elsevier Publishing Co., p. 676–685, New York.

    Google Scholar 

  • Johnson, C. A., Lvstad, R. A., Walaas, E., and Walaas, O., 1970, The properties of neuraminidase-treated crystalline ceruloplasmin, Experientia 26: 134–135.

    PubMed  CAS  Google Scholar 

  • Kasavina, B. S., and Kolchinskaya, T. A., 1966, Studies of the human thyroid in some pathological conditions, Clin. Chim. Acta 13: 685–693.

    PubMed  CAS  Google Scholar 

  • Kristjansson, F. K., and Cipera, J. D., 1963, The effect of sialidase on pig transferrins, Can. J. Biochem. Physiol. 41: 2523–2527.

    PubMed  CAS  Google Scholar 

  • Kunii, H., 1971, Inactivation of human chorionic gonadotropin extracted from chorionic tissue and serum by neuraminidase, Tohoku J. Exp. Med. 105: 317–325.

    PubMed  CAS  Google Scholar 

  • Laurell, C.-B., 1965, Effect of neuraminidase, acetone, and chloroform on α1-antitrypsins, Scand. J. Clin. Lab. Invest. 17: 297–298.

    PubMed  CAS  Google Scholar 

  • Lowy, P. H., Keighley, G., and Borsook, H., 1960, Inactivation of erythropoietin by neuraminidase and by mild substitution reactions, Nature 185: 102–103.

    PubMed  CAS  Google Scholar 

  • Main, A. R., Tarkan, E., Aull, J. L., and Soucie, W. G., 1972, Purification of horse serum cholinesterase by preparative Polyacrylamide gel electrophoresis, J. Biol. Chem. 247: 566–571.

    PubMed  CAS  Google Scholar 

  • Malashevich, E. V., 1970, Dependence of the sialic acid content in tissues on functional state of the hypophysis-adrenal systems, Ukr. Biokhim. Zh. 42: 56–59.

    PubMed  CAS  Google Scholar 

  • Margolis, F., and Feigelson, P., 1964, Atropinesterase, a sialoprotein, Biochim. Biophys. Acta 89: 357–360.

    PubMed  CAS  Google Scholar 

  • Marshall, J. S., Green, A. M., Pensky, J., Williams, S., Zinn, A., and Carlson, D. M., 1974, Measurement of circulating desialylated glycoproteins and correlation with hepatocellular damage, J. Clin. Invest. 54: 555–562.

    PubMed  CAS  Google Scholar 

  • Mester, L., Moczar, E., and Laki, K., 1963, Structure et rôle de la partie glucidique du fibrinogène et de la fibrine: Sur les liaisons des composeś glucidiques, Séance 256: 307–308.

    CAS  Google Scholar 

  • Morell, A. G., Van Den Hamer, C. J. A., Scheinberg, I. H., and Ashwell, G. A., 1966, Preparation of radioactive sialic acid-free ceruloplasmin labelled with tritium on terminal D-galactose residues, 1966, J. Biol. Chem. 241: 3745–3749.

    PubMed  CAS  Google Scholar 

  • Morell, A. G., Irvine, R. A., Steinlieb, I., Scheinberg, I. H., and Ashwell, G., 1968, Physical and chemical studies on ceruloplasmin, J. Biol. Chem. 243: 155–159.

    PubMed  CAS  Google Scholar 

  • Morell, A. G., Gregoriadis, G., Scheinberg, I. H., Hickman, J., and Ashwell, G., 1971, The role of sialic acid in determining the survival of glycoproteins in the circulation, J. Biol. Chem. 246: 1461–1467.

    PubMed  CAS  Google Scholar 

  • Murthy, P. V. H., Raghupathy, E., and Chaikoff, I. L., 1965, Studies on thyroid proteins. I. Isolation and properties of a glycopeptide from sheep thyroglobulin, Biochem. 4: 611–618.

    Google Scholar 

  • Nelsestuen, G. L., and Suttie, J. W., 1971, Properties of asialo and aglycoprothrombin, Biochem. Biophys. Res. Commun. 45: 198–203.

    PubMed  CAS  Google Scholar 

  • Niedermeier, W. Schrohenloher, R. E., and Hurst, M., 1972, The localization of oligosaccharides in a human IgM protein, J. Immunol. 108: 346–351.

    PubMed  CAS  Google Scholar 

  • Nolan, C., and Smith, E. L., 1962, Glycopeptides. II. Isolation and properties of glycopeptides from rabbit γ-globulin, J. Biol. Chem. 237: 446–452.

    PubMed  CAS  Google Scholar 

  • Oshiro, Y., and Eylar, E. H., 1968, Physical and chemical studies on glycoproteins. III. The microheterogeneity of fetuin, a fetal calf serum glycoprotein, Arch. Biochem. Biophys. 127: 476–489.

    PubMed  CAS  Google Scholar 

  • Parker, W. C., and Beam, A. G., 1962, Studies on the transferrins of adult serum, cord serum, and cerebrospinal fluid: The effect of neuraminidase, J. Exp. Med. 115: 83–105.

    PubMed  CAS  Google Scholar 

  • Pepper, D. S., 1968, The sialic acids of horse serum with special reference to their virus inhibitor properties, Biochim. Biophys. Acta 156: 317–326.

    PubMed  CAS  Google Scholar 

  • Perona, G., Cortesi, S., Xodo, P., Scandellari, C., Ghiotto, G., and de Sandre, G., 1964, Variations of in vivo survival, acetylcholinesterase activity and sensitivity to acid lysis in human erythrocytes treated with proteolytic enzymes and neuraminidase, Acta Istopocia 4: 287–295.

    CAS  Google Scholar 

  • Pidemsky, E. L., and Afonina, T. D., 1970, The effect of some antiphlogistic preparations on the content of mucopolysaccharides in the blood and liver homogenates, Patol. Fizioli Eksp. Ter. 14: 74–76.

    Google Scholar 

  • Pricer, W. E., and Ashwell, G., 1971, The binding of desialylated glycoproteins by plasma membranes of rat liver, J. Biol. Chem. 246: 4825–4833.

    PubMed  CAS  Google Scholar 

  • Rao, V. S., and Sirsi, M., 1970, Serum sialic acid in rats bearing yoshida ascites sarcoma, Ind. J. Biochem. 7: 184–186.

    CAS  Google Scholar 

  • Regoeczi, E., and Hatton, M. W. C., 1974, Studies of the metabolism of asialotransferrins: The mechanism for the hypercatabolism of human asialotransferrin in the rabbit, Can. J. Biochem. 52: 645–651.

    PubMed  CAS  Google Scholar 

  • Regoeczi, E., Hatton, M. W. C., and Wong, K.-L., 1974, Studies of the metabolism of asialotransferrins: Potentiation of the catabolism of human asialotransferrin in the rabbit, Can. J. Biochem. 52: 155–161.

    PubMed  CAS  Google Scholar 

  • Robinson, J. C., and Pierce, J. E., 1964, Studies on inherited variants of blood proteins. III. Sequential action of neuraminidase and galactose oxidase on transferrin B1–2b2, Arch. Biochem. Biophys. 106: 348–352.

    PubMed  CAS  Google Scholar 

  • Robinson, J. C., and Pierce, J. E., 1964, Differential action of neuraminidase on human serum alkaline phosphatases, Nature 204: 472–473.

    PubMed  CAS  Google Scholar 

  • Robinson, J. C., Pierce, J. E., and Blumberg, B. S., 1966, The serum alkaline phosphatase of pregnancy, Am. J. Obst. Gynec. 94: 559–565.

    CAS  Google Scholar 

  • Rogers, J. C., and Kornfeld, S., 1971, Hepatic uptake of proteins coupled to fetuin glycopeptide, Biochem. Biophys. Res. Commun., 45: 622–629.

    PubMed  CAS  Google Scholar 

  • Rule, A. H., and Boyd, W. C., 1964, Relationships between blood group agglutinogens: Role of sialic acids, Transfusion 4: 449–456.

    PubMed  CAS  Google Scholar 

  • Sairam, M. R., and Moudgal, N. R., 1971, On the mechanism of action of the monkey urinary follicle stimulating hormone inhibitor—Its sialidase activity, Ind. J. Biochem. Biophys. 8: 141–146.

    CAS  Google Scholar 

  • Scharmann, W., Brückler, J., and Blobel, H., 1971, Wirkung bakterieller Neuraminidasen auf Transferrin vom Menschen, Rind und Kaninchen, Biochim. Biophys. Acta 229: 136–142.

    PubMed  CAS  Google Scholar 

  • Schengrund, C.-L., Jensen, D., and Rosenberg, A., 1972, Localization of sialidase in the plasma membrane of rat liver cells, J. Biol. Chem., 247: 2742–2746.

    PubMed  CAS  Google Scholar 

  • Schmid, K., Burke, J. F., Debray-Sachs, M., and Tokita, K., 1964, Sialic acid-deficient α1-acid glycoprotein produced in certain pathological states, Nature 204: 75–76.

    PubMed  CAS  Google Scholar 

  • Schooley, J. C., and Garcia, J. F., 1971, The destruction by neuraminidase of the biological activity of erythropoietin when complexed with antierythropoietin, Proc. Soc. Exp. Biol. Med. 138: 66–68.

    PubMed  CAS  Google Scholar 

  • Schooley, J. C., and Mahlmann, L. J., 1971, Inhibition of the biologic activity of erythropoietin by neuraminidase in vivo, J. Lab. Clin. Med. 78: 765–770.

    PubMed  CAS  Google Scholar 

  • Schultze, H. E., 1958, Über Glykoproteine. Deut. Med. Wochschr. 83: 1742–1752.

    CAS  Google Scholar 

  • Schultze, H. E., Gollner, I., Heide, K., Schonenberger, M., and Schwick, G. Z., 1955, Zur Kenntnis der α-Globuline des menschlichen Normalserums, Z. Naturforsch. 106: 463–473.

    Google Scholar 

  • Schultze, H. E., Schmidtberger, R., and Haupt, H., 1958, Untersuchungen uber die gebundenen Kohlenhydrate in isolierten Plasmaproteiden, Biochem. Z. 329: 490–507.

    PubMed  CAS  Google Scholar 

  • Sharma, N. C., and Sur, B. K., 1967, Serum fucose and sialic acid levels in indian children and adults under normal and pathological conditions, Ind. J. Med. Res. 55: 380–384.

    CAS  Google Scholar 

  • Shetlar, M. R., Foster, J. V., Kelly, K. H., Shetlar, C. L., Bryan, R. S., and Everett, M. R., 1949, The serum polysaccharide level in malignancy and in other pathological conditions, Cancer Res. 9: 515–519.

    PubMed  CAS  Google Scholar 

  • Shome, B., Parlow, A. F., Ramirez, V. D., Elrick, H., and Pierce, J. G., 1968, Human and porcine thyrotropins: A comparison of electrophoretic and immunological properties with the bovine hormone, Arch. Biochem. Biophys. 103: 444–455.

    Google Scholar 

  • Shownkeen, R. C., Thomas, M. B., and Hartree, A. A., 1973, Sialic acid and tryptophan content of subunits of human pituitary luteinizing hormone, J. Endocrinol. 59: 201–202.

    PubMed  CAS  Google Scholar 

  • Shvartz, L. S., and Paukman, L. I., 1971, Diabetic angiopathies and mucopolysaccharide metabolism, Probl. Endocrinol. 17: 37–41.

    Google Scholar 

  • Singh, R., Sur, B. K., Agarwal, S. N., and Ramraju, B., 1967, Serum sialic acid in malignancy, Ind. J. Med. Res. 55: 270–273.

    CAS  Google Scholar 

  • Sjöholm, I., 1967, Biochemical studies on oxytocin and oxytocinase, Acta Pharm. Suedcica 4: 81–96.

    Google Scholar 

  • Spiegelberg, H. L., and Weigle, W. O., 1966, Studies on the catabolism of γ subunits and chains, J. Immunol. 95: 1034–1040.

    Google Scholar 

  • Spiro, R. G., 1960, Studies on fetuin, a glycoprotein of fetal serum I. Isolation, chemical composition, and physicochemical properties, J. Biol. Chem. 235: 2860–2869.

    PubMed  CAS  Google Scholar 

  • Spiro, R. G., 1970, Structure metabolism and biology of glycoproteins, Ann. Rev. Biochem. 39: 599–638.

    PubMed  CAS  Google Scholar 

  • Spiro, M. J., and Spiro, R. G., 1962, Composition of the peptide portion of fetuin, J. Biol. Chem. 237: 1507–1510.

    PubMed  CAS  Google Scholar 

  • Spiro, R. G., and Spiro, M. J., 1965, The carbohydrate composition of the thyroglobulins from several species, J. Biol. Chem. 240: 997–1001.

    PubMed  CAS  Google Scholar 

  • Spiro, M. J., and Spiro, R. G., 1968, Glycoprotein biosynthesis: Studies on thyroglobulin, J. Biol. Chem. 243: 6520–6528.

    PubMed  CAS  Google Scholar 

  • Stratel, A., and Spooner, R. L., 1971, Isolation and properties of individual components of cattle transferrin: The role of sialic acid, Biochem. Genetics 5: 347–365.

    Google Scholar 

  • Svensmark, O., 1961, Human-serum cholinesterase as a sialo-protein, Acta Physiol. Scand. 52: 267–275.

    PubMed  CAS  Google Scholar 

  • Svensmark, O., and Kristensen, P., 1962, Electrophoretic mobility of sialidase-treated human serum cholinesterase, Danish Med. Bull. 9: 16–17.

    PubMed  CAS  Google Scholar 

  • Svensmark, O., and Kristensen, P., 1963, Isoelectric point of native and sialidase-treated human-serum cholinesterase, Biochim. Biophys. Acta 67: 441–452.

    PubMed  CAS  Google Scholar 

  • Taoka, Y., and Fillios, L. C., 1971, Early effects of protein depletion on hepatic glycoprotein synthesis in the rat, J. Nutr. 101: 93–100.

    PubMed  CAS  Google Scholar 

  • Tuppy, H., Wiesbauer, U., and Wintersberger, E., 1963, Uber die Einwirkung von Neuraminidase auf die Serumoxytocinase, Mh. Chem. 94: 321–328.

    CAS  Google Scholar 

  • van den Hamer, C. J. A., Morell, A. G., Scheinberg, I. H., Hickman, J., and Ashwell, G., 1970, Physical and chemical studies on ceruloplasmin. IX. The role of galactosyl residues in the clearance of ceruloplasmin from the circulation, J. Biol. Chem. 245: 4397–4402.

    Google Scholar 

  • Vaitukaitis, J. L., and Ross, G. T., 1971, Altered biologic and immunologic activities of progressively desialylated human urinary FSH, J. Clin. Endocrinol. Metab. 33: 308–311.

    PubMed  CAS  Google Scholar 

  • Van Hall, E., Vaitukaitis, J. L., Ross, G. T., Hickman, J. W., and Ashwell, G., 1971, Immunological and biological activity of HCG following progressive desialylation, Endocrinology 88: 456–464.

    PubMed  Google Scholar 

  • Vermylen, J., Donati, M. B., de Gaetano, G., and Verstraete, M., 1973, Aggregation of human platelets by bovine or human factor. VIII: Role of carbohydrate side chains, Nat. New Biol. 244: 167–168.

    CAS  Google Scholar 

  • Vermylen, J., de Gaetano, G., Donati, M. B., and Verstraete, M., 1974, Plateletaggregating activity in neuraminidase-treated human cryoprecipitates: Its correlation with factor-VIII-related antigen. Br. J. Haematol. 26: 645–650.

    PubMed  CAS  Google Scholar 

  • Visser, A., and Emmelot, P., 1973, Studies on plasma membranes. XX. Sialidase in hepatic plasma membranes, J. Membrane Biol. 14: 73–84.

    CAS  Google Scholar 

  • Warren, L., 1959, The thiobarbituric acid assay of sialic acids, J. Biol. Chem. 234: 1971–1975.

    PubMed  CAS  Google Scholar 

  • Whitten, W. K., 1948, Inactivation of gonadotropins. II. Inactivation of pituitary and chorionic gonadotropins by influenza virus and receptor destroying enzyme, Austr. J. Sci. Res. B 1: 388–390.

    Google Scholar 

  • Winzler, R. J., 1955, Determination of Serum Glycoproteins. Methods of Biochemical Analysis. 2: 279–311.

    PubMed  CAS  Google Scholar 

  • Winzler, R., 1960, Glycoproteins, in: The Plasma Proteins (F. W. Putnam, ed.) pp. 309–347, Academic Press, New York.

    Google Scholar 

  • Winzler, R., 1971, Glycoproteins in disease in: Glycoproteins of Blood Cells and Plasma (G. A. Jamieson and T. J. Greenwalt, eds.), pp. 204–213, Lippincott Co., Philadelphia.

    Google Scholar 

  • Winzler, R., and Bocci, V., 1972, Turnover of plasma glycoproteins, in: Glycoproteins, Part B (A. Gottschalk, ed.), pp. 1228–1245, Elsevier Publishing Co., New York.

    Google Scholar 

  • Woodman, R. J., 1974, Carbocyanine dye metachromasia of sialidase-sensitive polyanions in sera from normal and tumor-bearing mice, Cancer Res. 34: 2897–2905.

    PubMed  CAS  Google Scholar 

  • Woodruff, J. J., and Gesner, B. M., 1969, The effects of neuraminidase on the fate of transfused lymphocytes, J. Exp. Med. 129: 551–567.

    PubMed  CAS  Google Scholar 

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  1. Department of Biological Chemistry, The Milton S. Hershey Medical Center, The Pennsylvania State University, Hershey, Pennsylvania, 17033, USA

    Abraham Rosenberg & Cara-Lynne Schengrund

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  2. Cara-Lynne Schengrund
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  1. Pennsylvania State University, Hershey, USA

    Abraham Rosenberg  & Cara-Lynne Schengrund  & 

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© 1976 Plenum Press, New York

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Rosenberg, A., Schengrund, CL. (1976). Circulating Sialyl Compounds. In: Rosenberg, A., Schengrund, CL. (eds) Biological Roles of Sialic Acid. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2226-9_9

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  • DOI: https://doi.org/10.1007/978-1-4684-2226-9_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-2228-3

  • Online ISBN: 978-1-4684-2226-9

  • eBook Packages: Springer Book Archive

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