Document Detail


The effect of chemical modification of basic amino acid residues on the activation and amidolytic activity of Hageman factor (factor XII).
MedLine Citation:
PMID:  8245689     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Modification of arginyl residues of Hageman factor by phenylglyoxal hydrate inhibits activation of this clotting factor in a plasma-free system, that is, in the absence of the other constituents of the contact activation system. Activation is also inhibited by alteration of the other two basic amino acid residues present, lysine and histidine. Chemical modification of histidine and arginine residues does not inhibit the amidolytic activity of activated Hageman factor. In contrast, modification of amino group(s) in N-terminal and lysine residues inhibits activated Hageman factor. Thus, basic amino acid residues essential to the activation or activity of Hageman factor appear to be variably accessible to chemical modification.
Authors:
J Ryder; B Everson; J Jentoft; O D Ratnoff
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of laboratory and clinical medicine     Volume:  122     ISSN:  0022-2143     ISO Abbreviation:  J. Lab. Clin. Med.     Publication Date:  1993 Dec 
Date Detail:
Created Date:  1994-01-04     Completed Date:  1994-01-04     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0375375     Medline TA:  J Lab Clin Med     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  697-702     Citation Subset:  AIM; IM    
Affiliation:
Department of Pathology, School of Medicine, Case Western Reserve University Cleveland, OH.
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MeSH Terms
Descriptor/Qualifier:
Amides / metabolism
Amino Acids / chemistry*
Arginine / chemistry
Diethyl Pyrocarbonate / pharmacology
Factor XII / antagonists & inhibitors,  chemistry*,  metabolism
Factor XIIa / metabolism
Histidine / chemistry
Humans
Lysine / chemistry
Phenylglyoxal / pharmacology
Serum Albumin, Bovine / pharmacology
Structure-Activity Relationship
Trinitrobenzenesulfonic Acid / pharmacology
Grant Support
ID/Acronym/Agency:
HL01661/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Amides; 0/Amino Acids; 0/Serum Albumin, Bovine; 1074-12-0/Phenylglyoxal; 1609-47-8/Diethyl Pyrocarbonate; 2508-19-2/Trinitrobenzenesulfonic Acid; 56-87-1/Lysine; 71-00-1/Histidine; 74-79-3/Arginine; 9001-30-3/Factor XII; EC 3.4.21.38/Factor XIIa

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


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