Linked Life Data

12759517

Source:http://linkedlifedata.com/resource/pubmed/id/12759517

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-5-21
pubmed:abstractText
We aimed at clarifying the structural characteristics of the bound thrombin that is liberated by mechanical breakdown of fibrin clots. Fibrin clots were prepared with bovine thrombin and rabbit fibrinogen, and were crushed mechanically with a glass rod. The supernatant of the crushed clots was subjected to immunoaffinity chromatography to isolate the bound thrombin. Western blotting analysis revealed that the bound thrombin could be reacted with both antithrombin and antifibrinogen under unreduced conditions. SDS-PAGE under reduced conditions revealed that there were three bands, two of which were found to be the N-terminal fragments of the alpha- and gamma-chains of fibrinogen. The bound thrombin could be dissociated into three distinct fibrin fragments and bovine alpha-thrombin when denatured by 8 M urea. Thus, the bound thrombin liberated from crushed clots is a stable complex between bovine alpha-thrombin and fibrin fragments of the N-terminal regions of rabbit alpha- and gamma-chains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1424-8832
pubmed:author
pubmed:copyrightInfo
Copyright 2002 S. Karger AG, Basel
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-73
pubmed:meshHeading
pubmed:articleTitle
Bound thrombin from crushed clots is composed of alpha-thrombin and the N-terminal regions of alpha- and gamma-chains of fibrinogen.
pubmed:affiliation
1st Department of Physiology, School of Medicine, University of the Ryukyus, Okinawa, Japan. physiol1@med.u-ryukyu.ac.jp
pubmed:publicationType
Journal Article