Open AccessPurification of a plasminogen activator from Streptococcus uberis
Author(s) -
Leigh J.A.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06818.x
Subject(s) - molecular mass , plasmin , streptococcus uberis , size exclusion chromatography , ammonium sulfate precipitation , plasminogen activator , monoclonal antibody , chemistry , antiserum , antibody , chromatography , affinity chromatography , microbiology and biotechnology , biochemistry , ammonium , biology , streptococcus , bacteria , immunology , endocrinology , organic chemistry , genetics , enzyme
A protein capable of activating bovine, equine and ovine plasminogen, but not that from human or porcine plasma, was purified from culture filtrates of Streptococcus uberis (strain 0140j). Purification was achieved by ammonium sulphate precipitation followed by molecular exclusion chromatography. The elution position of the native molecule was equivalent to a molecular mass of approximately 57 kDa. However, the molecular mass, as determined by SDS‐PAGE, was 29 kDa, suggesting the existence of a dimeric structure. Purified immunoglobulin from three out of five monoclonal antibodies raised to this protein inhibited the conversion of bovine plasminogen to plasmin by the purified protein.