Literature DB >> 877560

Formation of a serine enzyme in the presence of bovine factor VIII (antihemophilic factor) and thrombin.

G A Vehar, E W Davie.   

Abstract

Factor VIII is present in plasma in a precursor or inactive form. When bovine factor VIII that has been purified approximately 10,000-fold is incubated with thrombin, an activated product is formed which participates in the conversion of factor X to factor Xa in the presence of factor IXa, calcium ions, and phospholipid. This activated product, which has been tentatively identified as activated factor XIII, was stable when formed in the presence of 0.25M CaCl2 but was rapidly inactivated in the absence of CaCl2. It was inhibited by diisopropyl phosphorofluoridate and antithrombin III, suggesting that it is a serine enzyme. The exact role of this serine enzyme in the intrinsic pathway of coagulation remains to be established.

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Year:  1977        PMID: 877560     DOI: 10.1126/science.877560

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  2 in total

1.  Structural model of porcine factor VIII and factor VIIIa molecules based on scanning transmission electron microscope (STEM) images and STEM mass analysis.

Authors:  M W Mosesson; D N Fass; P Lollar; J P DiOrio; C G Parker; G J Knutson; J F Hainfeld; J S Wall
Journal:  J Clin Invest       Date:  1990-06       Impact factor: 14.808

2.  Disulfide bonds and the quaternary structure of factor VIII/von Willebrand factor.

Authors:  R B Counts; S L Paskell; S K Elgee
Journal:  J Clin Invest       Date:  1978-09       Impact factor: 14.808

  2 in total

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