Document Detail


Formation, characterization and detection of a ternary complex between S protein, thrombin and antithrombin III in serum.
MedLine Citation:
PMID:  3606566     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
S protein, a plasma glycoprotein with Mr 78,000, has been shown to interfere with the heparin-catalysed inhibition of thrombin by antithrombin III. This interaction was further evaluated in the present study. Native human blood was replaced by either radiolabelled antithrombin III or radiolabelled prothrombin in the reaction mixture, which was incubated at 37 degrees C. At various time intervals the serum formed from the incubated blood was withdrawn and analysed by crossed immunoelectrophoresis against anti-(S protein) serum in the second dimension. Increasing quantities of radioactivity originating both from antithrombin III and from thrombin were precipitated in a cathodal shoulder to the S protein peak. This observation indicated the formation of a ternary S protein-thrombin-antithrombin III (STAT) complex in serum. This complex could also be observed by the same technique after incubation of purified thrombin in the presence of antithrombin III and S protein. Complex-formation was independent of the presence of heparin and did not require Ca2+ ions. Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS. Both the serum-originated STAT complex and the STAT complex assembled from purified components sedimented faster than the single components and showed comparable apparent sedimentation coefficients in the range 11-14 S, corresponding to a mean Mr of 350,000. The STAT complex could be detected in serum at a dilution of 1:3200 by a sensitive immuno-radiometric assay employing affinity-purified IgG against S protein. These results indicate that S protein, in addition to its role as a heparin-neutralizing factor, becomes incorporated into the nascent TAT complex or can bind to preformed TAT complex during the clotting process.
Authors:
K T Preissner; L Zwicker; G Müller-Berghaus
Related Documents :
24817366 - Presence of a glycine-cysteine-rich beta-protein in the oberhautchen layer of snake epi...
9263726 - Activated protein c resistance--a major risk factor for thrombosis.
7600126 - Antithrombotic effects of activated protein c and protein s in a rabbit model of microa...
24999486 - Lysosomal abnormalities in hereditary spastic paraplegia types spg15 and spg11.
11350176 - The fast folding pathway in human lysozyme and its blockage by appropriate mutagenesis:...
11006546 - Modular evolution of the purine biosynthetic pathway.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  243     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1987 Apr 
Date Detail:
Created Date:  1987-08-14     Completed Date:  1987-08-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  105-11     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Antithrombin III / metabolism*
Centrifugation, Density Gradient
Electrophoresis, Polyacrylamide Gel
Glycoproteins / blood*
Humans
Immunoelectrophoresis
Macromolecular Substances
Membrane Glycoproteins*
Radioimmunoassay
Thrombin / metabolism*
Chemical
Reg. No./Substance:
0/Glycoproteins; 0/Macromolecular Substances; 0/Membrane Glycoproteins; 0/S-protein (control); 9000-94-6/Antithrombin III; EC 3.4.21.5/Thrombin
Comments/Corrections

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


Previous Document:  Characterization and genetic control of the prolamins of Haynaldia villosa: relationship to cultivat...
Next Document:  Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones.