Affiliation:
1. Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan
Abstract
Inniss, William
E. (Michigan State University, East Lansing)
and Charles L. SanClemente
. Biochemical studies on staphylocoagulase and an allied phosphatase activity. J. Bacteriol.
83:
941–947. 1962.—The present investigation was undertaken to determine whether the reported correlation between the coagulase and phosphatase activity of the staphylococci was functional.
Staphylococcus aureus
, phage-propagating strain 70, grown in brain heart infusion was the source of the purified coagulase. The concomitant phosphatase activity, measured spectrophotometrically at 400 mμ using
p
-nitrophenylphosphate as substrate, showed a parallel decrease during thermal inactivation at 37 and 56 C. Anion-exchange chromatography and electrophoresis using starch, starch gel, and paper as stabilizing media failed to separate the two activities. Since iodoacetate, ethylenediamine-tetraacetate, fluoride, azide, and
p
-chloromercuribenzoate always exerted different degrees of inactivation, apparently the same mechanism was not involved. This supposition was supported by subsequent saturation of the phosphatase with excess substrate (100-fold K
s
value) and the demonstration that under this condition coagulase was not inhibited. During this purification process, comparable increases in specific activity occurred for both coagulase and phosphatase, indicating the presence of a common protein carrier.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
5 articles.
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