The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 106, 439-453, Copyright, 1957, by The Rockefeller Institute for Medical Research New York

ARTICLE

THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE

Leonard T. Skeggs Jr. Ph.D.1, Joseph R. Kahn M.D.1, Kenneth Lentz Ph.D.1, and Norman P. Shumway M.D.1

1 From the Department of Medicine and Surgery, Veterans Administration Hospital, and the Department of Pathology, Western Reserve University, Cleveland

A purified preparation of a polypeptide renin substrate prepared by tryptic degradation of the protein renin substrate has been analyzed by the fluorodinitrobenzene method and after degradation with renin, carboxypeptidase, and phenylisothiocyanate, has been found to possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser. The first 10 of these amino acids constitutes hypertensin I which is released by cleavage of the leucyl-leucine bond by renin. The remaining 4 amino acids, leu, val, tyr, ser, apparently link hypertensin I to the protein renin substrate.

Submitted on April 14, 1957


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