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Studies on Glycopeptide Released by Trypsin from Sheep Erythrocytes

From the Department of Internal Medicine and Biochemistry, Kanazawa University School of Medicine, Kanazawa, Japan

Abstract

Pretreatment of sheep erythrocytes with trypsin abolishes their specific binding and rosette formation with human T lymphocytes. A glycopeptide containing sialic acid is released from the intact sheep erythrocytes by incubation with trypsin and purified. This glycopeptide contains activity that can be bound to T lymphocytes and produces inhibition of rosette formation. This component with a m.w. of about 10,000 contains galactose, acetylglucosamine, acetylgalactosamine, sialic acid, and serine. These results suggest that the glycopeptide released by trypsin treatment may contain the site of the T cell receptor of sheep erythrocytes.