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Research Abstract

Studies on glycopeptide released by trypsin from sheep erythrocytes.

Kitao T, Takeshita M, Hattori K
Journal of immunology (Baltimore, Md. : 1950)
Jul 1, 1976
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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.

External References

PubMed ID:
932429

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