Detection and characterization of extracellular proteases in Butyrivibrio fibrisolvens H17c View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-06

AUTHORS

Eldie Strydom, Rod I. Mackie, David R. Woods

ABSTRACT

The detection and approximate molecular weights of extracellular serine protease isoenzymes produced by Butyrivibrio fibrisolvens H17c were determined by gelatin-PAGE. Nine bands of protease activity with apparent molecular weights of approximately 101000, 95000, 87000, 80000, 76000, 68000, 63000, 54000 and 42000 were detected after gelatin-PAGE of supernatants from exponential phase cultures. A tenth serine protease band with an apparent molecular weight of approximately 32000 was detected in stationary phase cells. The activities of all ten protease bands were inhibited by a serine protease inhibitor but their activities were not affected by inhibitors of trypsin-like enzymes or metallo-, sulphydryl-and carboxylproteases. The activity of all ten exoprotease bands was optimal between pH 6.0 and 7.5. The ten exoprotease bands were only detected in media containing trypticase or casamino acids as nitrogen sources. Production of the ten protease bands was not affected by the carbohydrate source. More... »

PAGES

214-217

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00261539

DOI

http://dx.doi.org/10.1007/bf00261539

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048266028


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