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Isolation and Complete Amino Acid Sequence of Human Thymopoietin and Splenin

Tapan Audhya, David H. Schlesinger and Gideon Goldstein
Proceedings of the National Academy of Sciences of the United States of America
Vol. 84, No. 11 (Jun. 1, 1987), pp. 3545-3549
Stable URL: http://www.jstor.org/stable/29434
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Isolation and Complete Amino Acid Sequence of Human Thymopoietin and Splenin
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Abstract

Human thymopoietin and splenin were isolated from human thymus and spleen, respectively, by monitoring tissue fractionation with a bovine thymopoietin RIA cross-reactive with human thymopoietin and splenin. Bovine thymopoietin and splenin are 49-amino acid polypeptides that differ by only 2 amino acids at positions 34 and 43; the change at position 34 in the active-site region changes the receptor specificities and biological activities. The complete amino acid sequences of purified human thymopoietin and splenin were determined and shown to be 48-amino acid polypeptides differing at four positions. Ten amino acids, constant within each species for thymopoietin and splenin, differ between the human and bovine polypeptides. The pentapeptide active site of thymopoietin (residues 32-36) is constant between the human and bovine thymopoietins, but position 34 in the active site of splenin has changed from glutamic acid in bovine splenin to alanine in human splenin, accounting for the biological activity of the human but not the bovine splenin on the human T-cell line MOLT-4.

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