Isolation and characterization of a unique protease from sporulating cells of Bacillus subtilis.

Abstract:

:Two proteases, designated I and II, have been isolated from sporulating cells of Bacillus subtilis. They were partially purified by ammonium sulfate fractionation, Sephadex chromatography and affinity columns. Protease I was found to be similar to an already characterized B. subtilis protease. Protease II is trypsin-like in its substrate specificity and is distinct from protease I in its pH optimum, pH stability, molecular weight, substrate specificity, heat stability and sensitivity to various inhibitors. While both enzymes were produced primarily during sporulation, they attained maximum levels of activity at different times. Distinct functions for these proteases in post exponential B. subtilis are likely.

journal_name

Arch Microbiol

journal_title

Archives of microbiology

authors

Srivastava OP,Aronson AI

doi

10.1007/BF00425256

subject

Has Abstract

pub_date

1981-05-01 00:00:00

pages

227-32

issue

3

eissn

0302-8933

issn

1432-072X

journal_volume

129

pub_type

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