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Cooperativity of thymopoietin 32-36 (the active site) and thymopoietin 38-45 in receptor binding.

作者信息

Audhya T, Heavner G A, Kroon D J, Goldstein G

出版信息

Regul Pept. 1984 Oct;9(3):155-64. doi: 10.1016/0167-0115(84)90068-5.

Abstract

Thymopoietin is a 49 amino acid polypeptide hormone of the thymus whose biological activity is reproduced by the synthetic pentapeptide thymopentin, corresponding to amino acids 32-36. Thymopentin requires the addition of an octapeptide corresponding to thymopoietin 38-45 for full competition with native thymopoietin in a radioreceptor assay with receptor derived from the human T-cell line CEM. Thus thymopoietin appears to bind to its receptor on T-cells by two regions (32-36 and 38-45). Thymopentin alone is biologically active and induces elevations of intracellular cyclic GMP. Whilst occupancy of the adjacent site by thymopoietin 37-45 does not of itself cause an elevation of intracellular cyclic GMP this peptide is not biologically silent as it does enhance the potency of thymopentin.

摘要

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