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

Author:

Skeggs Leonard T.1,Kahn Joseph R.1,Lentz Kenneth1,Shumway Norman P.1

Affiliation:

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

Abstract

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.

Publisher

Rockefeller University Press

Subject

Immunology,Immunology and Allergy

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