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

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;...

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Detalles Bibliográficos
Autores principales: Skeggs, Leonard T., Kahn, Joseph R., Lentz, Kenneth, Shumway, Norman P.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1957
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136772/
https://www.ncbi.nlm.nih.gov/pubmed/13463253
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author Skeggs, Leonard T.
Kahn, Joseph R.
Lentz, Kenneth
Shumway, Norman P.
author_facet Skeggs, Leonard T.
Kahn, Joseph R.
Lentz, Kenneth
Shumway, Norman P.
author_sort Skeggs, Leonard T.
collection PubMed
description 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.
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spelling pubmed-21367722008-04-17 THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE Skeggs, Leonard T. Kahn, Joseph R. Lentz, Kenneth Shumway, Norman P. J Exp Med Article 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. The Rockefeller University Press 1957-09-01 /pmc/articles/PMC2136772/ /pubmed/13463253 Text en Copyright © Copyright, 1957, by The Rockefeller Institute for Medical Research New York This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Skeggs, Leonard T.
Kahn, Joseph R.
Lentz, Kenneth
Shumway, Norman P.
THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
title THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
title_full THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
title_fullStr THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
title_full_unstemmed THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
title_short THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
title_sort preparation, purification, and amino acid sequence of a polypeptide renin substrate
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136772/
https://www.ncbi.nlm.nih.gov/pubmed/13463253
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