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J. Biochem, 1982, Vol. 91, No. 6 1829-1836
© 1982 Japanese Biochemical Society

research-article

Glycophorins of Bovine Erythrocyte Membranes. Isolation and Preliminary Characterization of the Major Component1

Jun-Ichifo MURAYAMA, Motowo TOMTTA and Akira HAMADA

School of Pharmaceutical Sciences, Showa University Hatanodai, Stunagawa-ku, Tokyo 142

Crude glycophorin fraction was prepared from bovine erythrocyte membranes by extraction with lithium diiodosalicylate and partition in aqueous phenol. The crude fraction was further separated into three fractions by gel chromatography and ion-exchange chromatography. The major fraction, designated glycophorin BA, accounts for 80 % of the crude fraction. Its carbohydrate content was 79 % by weight including galactose, N-acetylgalactosamine, N-acetylglucosamine and N-glycorylneu-raminic acid. odosobenzoate treatment of glycophorin BA produced two fragments; one is a highly glycosylated segment and the other a hydrophobic peptide. The amino-terminal sequence of the hydrophobic peptide representing the carboxyl-terminal half of glycophorin BA was determined.

The other two fractions, IIIa and IIIb, were still heterogeneous when analyzed by gel electrophoresis. Fraction Ella contained two glycophorins having apparent molecular weights of 46,000 and 42,000, while fraction III contained a glycoprotein having a marked tendency to aggregate.

1This research was supported by a grant from the Ministry of Education, Science and Culture of Japan.


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