Biopolym. Cell. 1998; 14(2):152-155.
Structure and Function of Biopolymers
A comparative study of carbohydrate component of hen and human glycophorins
1Stasyk T. V., 2Krotkiewski H., 1Lutsik-Kordovsky M. D.
  1. Division of Cell Regulatory Systems of O.V. Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine
    14/16, Drahomanov Str., Lviv, Ukraine, 79005
  2. Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences
    R. Weigla 12, 53-114 Wroclaw, Poland


Sialoglycoproteins (SGPs) from plasma membranes of hen red blood cells were isolated by preparative SDS-PAGE and their carbohydrate composition and some immunochemical properties were investigated and compared with that of human glycophorin A. It was shown, that two principal SGPs with molecular weights of 28 kDa and 55 kDa are monomeric and dimeric forms of the same molecule and are immunochemically closely related. The amount of carbohydrate component consists about 33 % of molecular mass (in human glycophorin A it is 52.3 %). The analysis of monosaccharide composition of hen SGPs indicates, that they possess O-linked and N-linked oligocaccharide chains. In comparison with human glycophorin A hen SGPs have a higher amount of N-glycosidic chains and lower amount of O-glycosidic chains, the last are tentatively of more branched structure.


[1] Lisowska E. Antigenic properties of human erythrocyte glycophorins. Molecular immunology of complex carbohydrates. Ed. A. M. Wu. New York and London: Plenum press, 1988: 265-315.
[2] Cartron JP, Rahuel C. Human erythrocyte glycophorins: protein and gene structure analyses. Transfus Med Rev. 1992;6(2):63-92.
[3] Krotkiewski H. The structure of glycophorins of animal erythrocytes. Glycoconj J. 1988;5(1):35–48.
[4] Huang CH, Xie SS, Socha W, Blumenfeld OO. Sequence diversification and exon inactivation in the glycophorin A gene family from chimpanzee to human. J Mol Evol. 1995;41(4):478-86.
[5] Stasyk TV, Lutsik-Kordovsky MD. Isolation and properties of glycophorin from plasma membrane of hen red blood cells. Biopolym Cell. 1996; 12(4):94-9.
[6] Hamaguchi H, Cleve H. Solubilization and comparative analysis of mammalian erythrocyte membrane glycoproteins. Biochem Biophys Res Commun. 1972;47(2):459-64.
[7] Lutsyk MD, Oleshko PS, Tsegelskiy AA. Preparation and partial characterization of water-soluble membrane glycoprotein-lectin receptors. Biol membrany. 1992. 9(10-11):1025-7.
[8] Lutsyk MD, Oleshko PS, Vovkanych AS. [Electroelution of protein fractions from a polyacrylamide gel]. Ukr Biokhim Zh. 1990;62(1):112-5.
[9] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[10] Lutsik MD, Kusen' SI. [Study of membrane glycoproteins of human erythrocytes using lectins]. Ukr Biokhim Zh. 1987;59(6):3-9.
[11] Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979;76(9):4350-4.
[12] Nakane PK, Kawaoi A. Peroxidase-labeled antibody. A new method of conjugation. J Histochem Cytochem. 1974;22(12):1084-91.
[13] Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193(1):265-75.
[14] Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985;150(1):76-85.
[15] Jourdian GW, Dean L, Roseman S. The sialic acids. XI. A periodate-resorcinol method for the quantitative estimation of free sialic acids and their glycosides. J Biol Chem. 1971;246(2):430-5.
[16] Sawardeker JS, Sloneker JH, Jeanes A. Quantitative Determination of Monosaccharides as Their Alditol Acetates by Gas Liquid Chromatography. Anal Chem. 1965;37(12):1602–4.
[17] Fukuda M. Leukosialin, a major O -glycan-containing sialoglycoprotein defining leukocyte differentiation and malignancy. Glycobiology. 1991;1(4):347–56.