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Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A
We report the isolation and purification of the nephritis strain- associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1986
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188047/ https://www.ncbi.nlm.nih.gov/pubmed/3512759 |
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collection | PubMed |
description | We report the isolation and purification of the nephritis strain- associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed that NSAP could act as a plasminogen activator; immunological investigations indicated that NSAP is antigenically different from streptokinase from group C streptococcus, and possibly represents a unique streptokinase. It is this uniqueness that may contribute to the role of NSAP in the pathogenesis of acute poststreptococcal glomerulonephritis. |
format | Text |
id | pubmed-2188047 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1986 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21880472008-04-17 Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A J Exp Med Articles We report the isolation and purification of the nephritis strain- associated protein (NSAP) first described by Villareal et al. (8). Amino acid analysis, and determination of the first 21 amino-terminal amino acids indicated that this 46 kD protein is a streptokinase. Biochemical analysis confirmed that NSAP could act as a plasminogen activator; immunological investigations indicated that NSAP is antigenically different from streptokinase from group C streptococcus, and possibly represents a unique streptokinase. It is this uniqueness that may contribute to the role of NSAP in the pathogenesis of acute poststreptococcal glomerulonephritis. The Rockefeller University Press 1986-03-01 /pmc/articles/PMC2188047/ /pubmed/3512759 Text en 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 | Articles Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A |
title | Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A |
title_full | Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A |
title_fullStr | Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A |
title_full_unstemmed | Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A |
title_short | Purification and partial characterization of the nephritis strain- associated protein from Streptococcus pyogenes, group A |
title_sort | purification and partial characterization of the nephritis strain- associated protein from streptococcus pyogenes, group a |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188047/ https://www.ncbi.nlm.nih.gov/pubmed/3512759 |