Biopolym. Cell. 1996; 12(4):94-99.
Isolation and properties of glycophorin from plasma membrane of hen red blood cells
1Stasyk T. V., 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


Membrane glycoproteins of hen red blood cells were obtained by extraction of isolated membranes with chloroform – isopropanol mixture. Polyacrylamide slab gel electrophoresis in the presence of DS-Na revealed several major fractions with molecular weights 28,55,130,140,155 kDa and minor fractions with M. W. 22, 40, 50 kDa. Specific to O-glycosidic chains peanut and jack fruit lectins bound with<28 kDa and 55 kDa bands. Sialoglycoproteins with M. W. 28 kDa and 55 kDa were obtained in pure state by preparative electrophoresis. After subsequent electrophoresis of 55 kDa glycoprotein besides the main band 55 kDa fraction with M. W. 28 kDa was revealed. It is suggested that glycoprotein with M. W. 55 kDa is a dimeric form of 28 kDa glycoprotein. Sialoglycoprotein 28 kDa interacted with lectins of peanut, jack fruit, wheat germ, castor bean, lentil, red kidney bean, garden snail, laburnum anagyroides bark and did not bind concanavalin A. The properties of Sialoglycoproteins with M. W. 28 kDaand 55 kDa resemble that of human and mammalian glycophorins.


[1] Cartron JP, Rahuel C. Human erythrocyte glycophorins: protein and gene structure analyses. Transfus Med Rev. 1992;6(2):63-92.
[2] Krotkiewski H. The structure of glycophorins of animal erythrocytes. Glycoconjugate J. 1988;5(1):35–48.
[3] Rearden A, Magnet A, Kudo S, Fukuda M. Glycophorin B and glycophorin E genes arose from the glycophorin A ancestral gene via two duplications during primate evolution. J Biol Chem. 1993;268(3):2260-7.
[4] Weise MJ, Ingram VM. Proteins and glycoproteins of membranes from developing chick red cells. J Biol Chem. 1976;251(21):6667-73.
[5] Hamaguchi H, Cleve H. Solubilization and comparative analysis of mammalian erythrocyte membrane glycoproteins. Biochem Biophys Res Commun. 1972;47(2):459-64.
[6] Lutsik MD, Oleshko YaS, Tsegel'skiy AA. Preparation and partial characterization of water-soluble membrane glycoprotein-lectin receptors. Biol Membrany. 1992. 9(10-11):1025-7.
[7] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[8] Lutsik MD, Kusen' SI. Study of membrane glycoproteins of human erythrocytes using lectins. Ukr Biokhim Zh. 1987;59(6):3-9.
[9] 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.
[10] Lutsyk MD, Oleshko PS, Vovkanych AS. Electroelution of protein fractions from a polyacrylamide gel. Ukr Biokhim Zh. 1990;62(1):112-5.
[11] Kleinzeller A. Cukry a jejich derivaty. Laboratorni technika biochemie. Ed. F. Sorm. Praha: Ceskoslov. Akad. Ved., 1959. 501 p.
[12] 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.
[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] Chan LL. Changes in the composition of plasma membrane proteins during differentiation of embryonic chick erythroid cell. Proc Natl Acad Sci U S A. 1977;74(3):1062-6.