Biopolym. Cell. 1996; 12(4):94-99.
http://dx.doi.org/10.7124/bc.00043F
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

Abstract

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.
Full text: (PDF, in Ukrainian)

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