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Structural Concepts of the Human Blood Group A, B, H, Lea, Leb, I and i Active Glycoproteins Purified from Human Ovarian Cyst Fluid

  • Albert M. Wu
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 228)

Abstract

The chemical structures of the blood group A, B, H, Lea, Leb, I and i determinants in water soluble blood group substances isolated from human ovarian cyst fluid have been studied for over four decades and are well established (1–10). However, the internal structure of the carbohydrate moiety had not been approached until base was applied to cleave the o- glycosidic linkage between the GaAc of the carbohydrate moiety and Thr and Ser of the protein core (8,11–15). The proposed composite structure of the carbohydrate side chains of blood group A, B, H, Lea and Leb substances (5,16,17) and of precursor substances with I and i determinants (18) shown in Fig. 1 were inferred from the mechanism of the alkaline ß-elimination and peeling reactions, together with the structures of the oligosaccharide fragments isolated (16) . More evidence is needed to confirm these carbohydrate internal structures. ß-elimination of intact blood group substances Fig. 1 (A) Proposed composite oligosaccharide structure (2,16,19) showing the relationship of the various blood group determinants and genes involved. Asterisk denotes that A substances have not been examined for oligosaccharides in this region (17).

Keywords

Blood Group High Pressure Liquid Chromatography Carbohydrate Chain Immunochemical Study Specific Lectin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

GalNAc

2-acetamido-2-deoxy-D-galactopyranose

Gal

D-galactopyranose

Fuc or LFuc

L-fucopyranose

GlcNAc

2-acetamido-2-deoxy-D-glucopyranose

GalNAc-ol

2-acetamido-2-deoxy-Dgalactitol

Gal-ol

galactitol

GLC-MS

gas-liquid chromatography-mass spectrometry

HPLC

high pressure liquid chromatography

FAB

fast atom bombardment

NOE

nuclear Overhauser enchancement

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References

  1. 1.
    Watkins, W.M. (1980) Biochemistry and Genetics of the ABO, Lewis, and P Blood Group System Advan. Hum. Genet., 10:1–136.Google Scholar
  2. 2.
    Kabat, E.A. (1976) Antibody (and Lectin) Combining Sites for Elucidation of Structures of Antigenic Determinant. Structural Concepts in Immunology and Immunochemistry, 2nd ed., pp 167–200, Holt, Rinehart & Winston, New York.Google Scholar
  3. 3.
    Lloyd, K.O.(1976) Glycoproteins with blood group activity. International Review of Science Organic Chemistry Series Two, Vol. 7, Carbohydrates, (Aspinall, G.O., ed.) pp 251–281, London, Butterworths.Google Scholar
  4. 4.
    Watkins, W.M. (1972) Blood Group Specific Substance In Glycoproteins, (Gottschalk, A., ed.) 2nd ed., pp. 883–891, Elsevier, Amsterdam.Google Scholar
  5. 5.
    Rovis, L., Anderson, B., Rabat, E.A., Gruezo, F., and Liao, J. (1973) Structures of oligosaccharides produced by base-borohydride degradation of human ovarian cyst blood group H, Leb, and Lea active glycoproteins. Biochemistry, 12:5340–5354.PubMedCrossRefGoogle Scholar
  6. 6.
    Schiffman, G., Kabat, E.A., and Leskowitz, S. (1960) Immunochemical studies on blood groups. XXIV. Some oligosaccharides isolated from dialysates after mild acid hydrolysis of human blood group B substances from ovarian cyst fluid. J. Amer. Chem., Soc., 82:1122–1127.CrossRefGoogle Scholar
  7. 7.
    Schiffman, G., Kabat, E.A., and Leskowitz, S. (1962) Immunochemical studies on blood groups. XXVI. The isolation of oligosaccharides from human ovarian cyst blood group A substance including two disaccharides and a trisaccharide involved in the specificity of the blood group A antigenic determinant. J. Amer. Chem. Soc., 84:73–77.CrossRefGoogle Scholar
  8. 8.
    Morgan, W.T.J. (1960) The Croonian lecture. A contribution to human biochemical genetics; the chemical basis of blood group specificity. Proc. Royal Soc., Ser B., 151:308–347.CrossRefGoogle Scholar
  9. 9.
    Kabat, E.A. (1956) Blood Group Substances: Their Chemistry and Immunochemistry, pp 1–330, Academic Press, New York.Google Scholar
  10. 10.
    Watkins, W.M., Yates, A.D., and Greenwell, P. (1981) Blood group antigens and the enzymes involved in their synthesis: past and present. Biochem. Soc. Trans., 9:186–191.PubMedGoogle Scholar
  11. 11.
    Anderson, B., Hoffmann, P., and Meyer, K. (1964) A serine- linked peptide of chondroitin sulfate. Biochim. Biophys. Acta, 74:309–311.CrossRefGoogle Scholar
  12. 12.
    Schiffman, G., Kabat, E.A., and Thompson, W. (1964) Immunochemical studies on blood groups. XXX. Cleavage of A, B, and H blood-group substances by alkali. Biochemistry, 3:113–120.PubMedCrossRefGoogle Scholar
  13. 13.
    Rege, V.P., Painter, T.J., Watkins, W.M., and Morgan, W.T.J. (1964) Isolation of serologically active fucose- containing oligosaccahrides from human blood group H substance. Nature, 203:360–363.PubMedCrossRefGoogle Scholar
  14. 14.
    Kabat, E.A., Bassett, E.W., Pryzwansky, K., Lloyd, K.O., Kaplan, M.E., and Layug, E.J. (1965) Immunochemical studies on blood groups. XXXIII. The effects of alkaline borohydride and of alkali on blood group A, B, and H substances. Biochemistry, 4:1632–1638.PubMedCrossRefGoogle Scholar
  15. 15.
    Lloyd, K.O., Kabat, E.A., and Rosenfield, R.E. (1966) Immunochemical studies on blood groups. XXXV. The activity of fucose-containing oligosaccharides isolated from blood group A, B, and H substances by alkaline degradation. Biochemistry, 5:1502–1507.PubMedCrossRefGoogle Scholar
  16. 16.
    Lloyd, K.O. and Kabat, E.A. (1968) Immunochemical studies on blood groups. XLI. Proposed structures for the carbohydrate portion of blood group A, B, H, Lewisa and Lewisb substances. Proc. Nat. Acad. Sci., 61:1470–1477.PubMedCrossRefGoogle Scholar
  17. 17.
    Wu, A.M., Kabat, E.A., Pereira, M.E.A., Gruezo, F.G., and Liao, J. (1982) Immunochemical studies on blood group: the internal structure and immunological properties of water-soluble human blood group A substance studied by Smith degradation, liberation and fractionation of oligosaccharides and reaction with lectins. Arch. Biochem. Biophys., 215:390–404.PubMedCrossRefGoogle Scholar
  18. 18.
    Vicari, G. Kabat, E. A. (1970) Structures and activities of oligosaccharides produced by alkaline degradation of a blood group substance lacking A, B, H, Lea, and Leb specificities. Biochemistry, 9:3414–3421.PubMedCrossRefGoogle Scholar
  19. 19.
    Lloyd, K.O., Kabat, E.A., and Licerio, E. (1968) Immunochemical studies on blood groups. XXXVIII. Structures and activities of oligosaccharides produced by alkaline degradation of blood group Lewisa substance. Proposed structure of the carbohydrate chains of human blood group A, B, H, Lea, and Leb substances. Biochemistry, 7:2976–2990.PubMedCrossRefGoogle Scholar
  20. 20.
    Kabat, E.A. (1982) Philip Levine Award Lecture. Contributions of quantitative immunochemistry to knowledge of blood group A, B, H, Le, I and i antigens. J. Amer. Clin. Pathol., 78:281–292.Google Scholar
  21. 21.
    Anderson, B., Rovis, L., and Kabat, E.A. (1972) Immunochemical Studies on Blood Groups. LIII. A Study of various conditions of alkaline borohydride degradation on human and hog blood group substances and on known oligosaccharides. Arch. Biochem. Biophys., 148:304–314.PubMedCrossRefGoogle Scholar
  22. 21A.
    Wood, E., Hounsell, E.F., and Feizi, T. (1981) Preparative, affinity chromatography of sheep gastric-mucins having blood-group I i activity, and release of antigenically active oligosaccharides by alkaline-borohydride degradation. Carbohydr. Res., 90:269–282.CrossRefGoogle Scholar
  23. 22.
    Wu, A.M., Kabat, E.A., Nilsson, B., Zopf, D.A., Gruezo, F.G., and Liao, J. (1984) Immunochemical studies on blood groups. Purification and characterization of radioactive 3H -reduced di- to hexasaccharides produced by alkaline β- elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins. J. Biol. Chem., 259:7178–7186.PubMedGoogle Scholar
  24. 23.
    Mutsaers, J.H.G.M., Van Halbeek, H., Vliegenthart, J.F.G., Wu, A.M., and Kabat, E.A. (1986) Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy. Eur. J. Biochem., 157:139–146.PubMedCrossRefGoogle Scholar
  25. 24.
    Maisonrouge-Muliffe, F., and Kabat, E.A. (1976) Immunochemical studies on blood groups. Structures and immunochemical properties of oligosaccharides from two fractions of blood group substance from human ovarian cyst fluid differing in B, I, and i activities and reactivity toward concanavalin A. Arch. Biochem. Biophys., 175:90–113.CrossRefGoogle Scholar
  26. 25.
    Dua, V.K., Rao, B.N., Wu, S.S., Dube, V.E., and Bush, A.C. (1986) Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoprotein of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy. J. Biol. Chem., 261:1599–1608.PubMedGoogle Scholar
  27. 26.
    Dua, V.K., Dube, V.E., and Bush, A.C. (1984) The combination of normal-phase and reverse-phase high-pressure liquid chromatography with NMR for the isolation and characterization of oligosaccharide alditols from ovarian cyst mucins. Biochim. Biophys. Acta, 802:2 9–40.Google Scholar
  28. 27.
    Dua, V.K., Dube, V.E., Li, Y.T., and Bush, C.A. (1985) Reverse phase HPLC fractionation of the oligosaccharide alditols isolated from an I-active ovarian cyst mucin glycoprotein. Glycoconjugate J., 2:17–30.CrossRefGoogle Scholar
  29. 27A.
    A Bush, C.A., Yan, Z-Y., and Rao, B.N.N. (1986) Conformational energy calculations and proton nuclear Overhauser enhancements reveal a unique conformation for blood group A oligosaccharides. J. Amer. Chem. Soc., 108:6168–6173.CrossRefGoogle Scholar
  30. 28.
    Maisonrouge-Muliffe, F., Kabat, E.A. (1976) Immunochemical studies on blood groups LXIV. Fractionation, heterogeneity, and chemical and immunochemical properties of a blood group substance with B, I, and i activities purified from human ovarian cyst fluid. Arch. Biochem. Biophys., 175:71–80CrossRefGoogle Scholar
  31. 29.
    Zinn, AB.,Plantner, J.J.,and Carlson, D.M. (1977) Nature of linkage between protein core and oligosaccharides in The Glycoconjuates. Vol.1 (Horowitz, M.I. and Pigman, W., eds.) Academic Press, New York and London.Google Scholar
  32. 30.
    Feizi, T., Kabat, E.A., Vicari, G., Anderson B.,and Marsh, W.L. (1971) Immunochemical studies on blood groups XLVII. The I antigen complex-precursors in the A, B, H, Lea, and Leb blood group system-hemagglutination-inhibition studies. J. Exp. Med., 133:39–52.Google Scholar
  33. 31.
    Danishefsky, I., Whistler, R.L., and Bettelheim, (1970) Introduction to polysaccharide chemistry in The Carbohydrates, Chemistry and Biochemistry. 2nd ed. Vol. IIA, (Pigman, W. and Horton, D.,eds.) Academic Press, New York and London.Google Scholar
  34. 32.
    Marshall, R.D., and Neuberger, A. (1972) Structural Analysis of the Carbohydrate Groups of Glycoprotein in Glycoproteins, (Gottschalk, A., ed.) 2nd ed. Part A, pp.332–380, Elsevier, Amsterdam.Google Scholar
  35. 33.
    Wu, A.M., Wu, J.C., and Herp, A. (1978) Polypeptide linkages and resulting structural features as powerful chromogenic factors in the Lowry phenol reaction. Studies on a glycoprotein containing no Lowry phenol-reactive amino acids and on its desialylated and deglycosylated products. Biochem. J., 175:47–50.PubMedGoogle Scholar
  36. 34.
    Koerner, T.A.W., Yu, R.K., Scarsdale, J.N., Demou, P.C., and Prestegard, J.H. (1988) Analysis of complex carbohydrate primary and secondary structure via two- dimensional proton nuclear magnetic resonance spectroscopy,in The Molecular Immunology of Complex Carbohydrates, (Wu, A., ed.) IV-2, Plenum, New York and London.Google Scholar
  37. 35.
    Carr, S.A., Reinhold, V.N., Green, B.N., and Hass, J.R. (1985) Enhancement of structural information in FAB ionized carbohydrate samples by neutral gas collision. Biomed. Mass Spectrom., 12;288–295.PubMedCrossRefGoogle Scholar
  38. 36.
    Wu, A.M., and Sugii, S. (1988) Differential binding properties of GaAc and/or Gal specific lectins, in The Molecular Immunology of Complex Carbohydrates, (Wu, A. ed.) I–9, Plenum, New York and London.Google Scholar
  39. 37.
    Leskowitz, S. and Kabat, E.A.(1954) Immunochemical studies on blood groups XV. The effect of mild acid hydrolysis on the glucosamine and galactosamine° in blood group substances. J. Amer. Chem. Soc., 76:50 60–5065.Google Scholar
  40. 38.
    Allen, P.Z., and Kabat, E. A. (1959) Immunochemical studies on blood groups XXII. Immunochemical studies on the nondialyzable residue from partially hydrolyzed blood group A, B, and 0(H) substances (PI fractions). J. Immunol., 82:340–357.PubMedGoogle Scholar
  41. 39.
    Baker, D.A., Sugii, S., Kabat, E.A., Ratcliffe, R.M., Hermentin, P., and Lemieux, R.U. (1983) Immunochemical studies on the combining sites of Forssman hapten reactive hemagglutinins fromDolichos biflorus, Helix pomatia and Wistaria floribunda. Biochemistry, 22:2741–2750.PubMedCrossRefGoogle Scholar
  42. 40.
    Sarkar, M., Wu, A.M., and Kabat, E.A. (1981) Immunochemical studies on the carbohydrate specificity of Madura pomifera lectin. Arch. Biochem. Biophys., 209:204–218.PubMedCrossRefGoogle Scholar
  43. 41.
    Wu, A.M., Kabat, E.A., Gruezo, F.G., and Allen, H.J.(1980) Immunochemical studies on the combining site of the D-galactopyranose and 2-acetamido-2-deoxy-D-galact o- pyranose specific lectin isolated from Bauhinia purpurea alba seeds. Arch. Biochem. Biophys., 204:622–639.PubMedCrossRefGoogle Scholar
  44. 42.
    Wu, A.M., Kabat, E.A., Gruezo, F.G., and Poretz, R.D.(1981) Immunochemical studies on the reactivities and combining sites of the D-galactopyranose and 2-acetamido-2- deoxy-D-galactopyranose-specific lectin purified from Sophora japonica seeds. Arch. Biochem. Biophys., 209:191–203.PubMedCrossRefGoogle Scholar
  45. 43.
    Pereira, M.E.A., Kabat, E.A., Lotan, R., and Sharon, N. (1976) Immunochemical studies on the specificity of the peanut (Arachis hypogaea) agglutinin. Carbohydr. Res., 51:107–118.PubMedCrossRefGoogle Scholar
  46. 44.
    Wu, A.M., Sugii, S., Gruezo, F.G., and Kabat, E.A. (1987) Immunochemical studies on the Galβ1→4 (3) GlAc specificity of Ricinus communis agglutinin. Carbohydr. Res., (in press).Google Scholar
  47. 45.
    Bretting, H., Phillips, S.G., Klumpart, H.J., and Kabat, E.A. (1981) A mitogenic lactose-binding lectin from the spongeGeodia cydonium. J. Immmunol., 127:1652–1658.Google Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Albert M. Wu
    • 1
  1. 1.Department of Veterinary PathologyTexas A&M UniversityCollege StationUSA

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