THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE

Hog renin substrate has been separated into three major (A, B, and C) and two minor forms (D and E) by DEAE cellulose chromatography. Two of the major forms (B and C) have been further fractionated into two additional types (1 and 2) by countercurrent distribution. The purification of substrates A,...

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Detalles Bibliográficos
Autores principales: Skeggs, Leonard T., Lentz, Kenneth E., Hochstrasser, Harry, Kahn, Joseph R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1963
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137574/
https://www.ncbi.nlm.nih.gov/pubmed/13977879
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author Skeggs, Leonard T.
Lentz, Kenneth E.
Hochstrasser, Harry
Kahn, Joseph R.
author_facet Skeggs, Leonard T.
Lentz, Kenneth E.
Hochstrasser, Harry
Kahn, Joseph R.
author_sort Skeggs, Leonard T.
collection PubMed
description Hog renin substrate has been separated into three major (A, B, and C) and two minor forms (D and E) by DEAE cellulose chromatography. Two of the major forms (B and C) have been further fractionated into two additional types (1 and 2) by countercurrent distribution. The purification of substrates A, C(1), and C(2) has been completed. Analysis shows that all three are glycoproteins with molecular weights of about 57,000, and have similar amino acid compositions. Differences exist in the sialic acid, glucosamine, and neutral hexose content, which may account for different physical properties. All the forms of the substrates are attacked by renin at similar rates, and appear to yield the same angiotensin I.
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spelling pubmed-21375742008-04-17 THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE Skeggs, Leonard T. Lentz, Kenneth E. Hochstrasser, Harry Kahn, Joseph R. J Exp Med Article Hog renin substrate has been separated into three major (A, B, and C) and two minor forms (D and E) by DEAE cellulose chromatography. Two of the major forms (B and C) have been further fractionated into two additional types (1 and 2) by countercurrent distribution. The purification of substrates A, C(1), and C(2) has been completed. Analysis shows that all three are glycoproteins with molecular weights of about 57,000, and have similar amino acid compositions. Differences exist in the sialic acid, glucosamine, and neutral hexose content, which may account for different physical properties. All the forms of the substrates are attacked by renin at similar rates, and appear to yield the same angiotensin I. The Rockefeller University Press 1963-07-01 /pmc/articles/PMC2137574/ /pubmed/13977879 Text en Copyright © 1963, by The Rockefeller Institute 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.
Lentz, Kenneth E.
Hochstrasser, Harry
Kahn, Joseph R.
THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE
title THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE
title_full THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE
title_fullStr THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE
title_full_unstemmed THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE
title_short THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE
title_sort purification and partial characterization of several forms of hog renin substrate
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137574/
https://www.ncbi.nlm.nih.gov/pubmed/13977879
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