Literature DB >> 1167792

Purification and properties of staphylocoagulase.

B M Bas, A D Muller, H C Hemker.   

Abstract

Staphylocoagulase, an exoprotein of coagulase-positive Staphylococci, has been purified to a state in which only trace amounts of contaminating proteins are detectable. Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61 000; the isoelectric point lies as pH 4.53. The amino acid composition was determined.

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Year:  1975        PMID： 1167792     DOI： 10.1016/0005-2795(75)90018-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

1.  Adhesion of Staphylococcus aureus to the vessel wall under flow is mediated by von Willebrand factor-binding protein.

Authors:  Jorien Claes; Thomas Vanassche; Marijke Peetermans; Laurens Liesenborghs; Christophe Vandenbriele; Karen Vanhoorelbeke; Dominique Missiakas; Olaf Schneewind; Marc F Hoylaerts; Ruth Heying; Peter Verhamme
Journal:  Blood       Date:  2014-06-20       Impact factor: 22.113

2.  Dabigatran inhibits Staphylococcus aureus coagulase activity.

Authors:  Thomas Vanassche; Jan Verhaegen; Willy E Peetermans; Marc F Hoylaerts; Peter Verhamme
Journal:  J Clin Microbiol       Date:  2010-09-01       Impact factor: 5.948

3.  Partial purification and characterization of the multiple molecular forms of staphylococcal clotting activity (coagulase).

Authors:  M W Reeves; M C Drummond; M Tager
Journal:  J Bacteriol       Date:  1981-12       Impact factor: 3.490
  3 in total

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