PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION

The precursor of the kinin-forming enzyme, prekallikrein, was isolated from rabbit plasma protected from activation during preparatory procedures. Prekallikrein was shown to be a 4.5S γ(1)-glycoprotein with an isoelectric point of 5.9 and a mol wt of 99,900. The proenzyme was activated at neutral pH...

Descripción completa

Detalles Bibliográficos
Autores principales: Wuepper, Kirk D., Cochrane, Charles G.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1972
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139124/
https://www.ncbi.nlm.nih.gov/pubmed/4536682
_version_ 1782143723059019776
author Wuepper, Kirk D.
Cochrane, Charles G.
author_facet Wuepper, Kirk D.
Cochrane, Charles G.
author_sort Wuepper, Kirk D.
collection PubMed
description The precursor of the kinin-forming enzyme, prekallikrein, was isolated from rabbit plasma protected from activation during preparatory procedures. Prekallikrein was shown to be a 4.5S γ(1)-glycoprotein with an isoelectric point of 5.9 and a mol wt of 99,900. The proenzyme was activated at neutral pH by an enzyme from rabbit or human plasma we have termed prekallikrein activator (PKA) or by trypsin. Prekallikrein was activated by PKA by a process of enzymatic scission. This resulted in the appearance of two fragments; the larger of these possessed kallikrein activity.
format Text
id pubmed-2139124
institution National Center for Biotechnology Information
language English
publishDate 1972
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21391242008-04-17 PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION Wuepper, Kirk D. Cochrane, Charles G. J Exp Med Article The precursor of the kinin-forming enzyme, prekallikrein, was isolated from rabbit plasma protected from activation during preparatory procedures. Prekallikrein was shown to be a 4.5S γ(1)-glycoprotein with an isoelectric point of 5.9 and a mol wt of 99,900. The proenzyme was activated at neutral pH by an enzyme from rabbit or human plasma we have termed prekallikrein activator (PKA) or by trypsin. Prekallikrein was activated by PKA by a process of enzymatic scission. This resulted in the appearance of two fragments; the larger of these possessed kallikrein activity. The Rockefeller University Press 1972-01-01 /pmc/articles/PMC2139124/ /pubmed/4536682 Text en Copyright © 1972 by The Rockefeller University Press 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
Wuepper, Kirk D.
Cochrane, Charles G.
PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION
title PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION
title_full PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION
title_fullStr PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION
title_full_unstemmed PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION
title_short PLASMA PREKALLIKREIN: ISOLATION, CHARACTERIZATION, AND MECHANISM OF ACTIVATION
title_sort plasma prekallikrein: isolation, characterization, and mechanism of activation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139124/
https://www.ncbi.nlm.nih.gov/pubmed/4536682
work_keys_str_mv AT wuepperkirkd plasmaprekallikreinisolationcharacterizationandmechanismofactivation
AT cochranecharlesg plasmaprekallikreinisolationcharacterizationandmechanismofactivation

Ejemplares similares