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The fibrinolytic pathway of human plasma. Isolation and characterization of the plasminogen proactivator.
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MedLine Citation:
PMID:  4264575     Owner:  NLM     Status:  MEDLINE    
The conversion of the plasminogen proactivator to plasminogen activator by activated Hageman factor or its fragments has been recognized as an essential step in the conversion of plasminogen to plasmin. The plasminogen proactivator has been completely separated from prekallikrein and pre-PTA, two other proenzyme substrates of activated Hageman factor or its fragments. Plasminogen proactivator, free of any contaminating proteins as assessed by disc gel electrophoresis or isoelectric focusing, revealed a single band with an isoelectric point of 8.9 corresponding in position to the Hageman factor activatable material eluted from replicate unstained gels. After conversion of plasminogen proactivator by Hageman factor fragments to the plasminogen activator, the active site of the plasminogen activator is not inhibited by C1INH and is thus readily distinguished from that of kallikrein or PTA. The plasminogen activator is susceptible to inactivation by DFP while the plasminogen proactivator is not, as has been the case for esterases having a serine in the active site. Its interaction with plasminogen is inhibited by epsilon-aminocaproic acid.
A P Kaplan; K F Austen
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of experimental medicine     Volume:  136     ISSN:  0022-1007     ISO Abbreviation:  J. Exp. Med.     Publication Date:  1972 Dec 
Date Detail:
Created Date:  1973-02-17     Completed Date:  1973-02-17     Revised Date:  2010-06-22    
Medline Journal Info:
Nlm Unique ID:  2985109R     Medline TA:  J Exp Med     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1378-93     Citation Subset:  AIM; IM    
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MeSH Terms
Aminocaproic Acids / pharmacology
Blood Coagulation Factors* / isolation & purification
Chromatography, Gel
Complement System Proteins
Electrophoresis, Disc
Factor XII* / isolation & purification
Fibrinolysin* / antagonists & inhibitors
Histidine / antagonists & inhibitors
Isoelectric Focusing
Molecular Weight
Plasminogen / antagonists & inhibitors
Serine / antagonists & inhibitors
Reg. No./Substance:
0/Aminocaproic Acids; 0/Blood Coagulation Factors; 0/Kinins; 56-45-1/Serine; 71-00-1/Histidine; 9001-30-3/Factor XII; 9001-91-6/Plasminogen; 9007-36-7/Complement System Proteins; 9035-58-9/Thromboplastin; EC 3.4.-/Streptokinase; EC 3.4.21.-/Kallikreins; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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Journal Information
Journal ID (nlm-ta): J Exp Med
ISSN: 0022-1007
ISSN: 1540-9538
Publisher: The Rockefeller University Press
Article Information
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Copyright © 1972 by The Rockefeller University Press.
Received Day: 4 Month: 8 Year: 1972
Print publication date: Day: 30 Month: 11 Year: 1972
Volume: 136 Issue: 6
First Page: 1378 Last Page: 1393
ID: 2139321
PubMed Id: 4264575

Allen P. Kaplan
K. Frank Austen
From the Departments of Medicine, Harvard Medical School and Robert B. Brigham Hospital, Boston, Massachusetts 02120

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