Purification and some properties of the extracellular protease ofBacillus pumilus View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1970-05

AUTHORS

J. Fabián

ABSTRACT

Supernatant of a culture ofBacillus pumilus D 78 was precipitated with ethanol and chromatographed on DEAE- and CM-cellulose to isolate and purify a neutral protease with fibrinolytic and caseinolytic activity. Analysis by ultracentrifugation and immunoelectrophoresis indicate the homogeneity of the purified enzyme with the sedimentation constant s20,w equal to 2.3. The fibrinolytic activity had a lower heat stability and was also more sensitive to pH higher than 8.0. The caseinolytic activity was stable over a wide range of pH (4.5 to 11.0). The enzyme binds acid dyes and is inhibited by Cu2+, Zn2+, Ca2+ and Fe3+, as well as byL-cysteine and KCN at a concentration of 10mM. Likewise, EDTA andp-chloromercuribenzoate show an inhibitory effect. More... »

PAGES

169-175

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02873080

DOI

http://dx.doi.org/10.1007/bf02873080

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001033530

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4990355


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