Mar 11, 1976

Characterization of intracellular esterase A from Bacillus subtilis

Biochimica Et Biophysica Acta
J F Riefler, T B Higerd

Abstract

Esterase A (EC 3.1.1.1) obtained by sonic disruption of Bacillus subtilis SR22 (spoA12, trpC2) was purified approximately 400-fold by differential chemical and heating precipitation, DEAE-cellulose chromatography, and Bio-Rad P-150 gel filtration chromatography, with an overall yield of 59%. The purified enzyme hydrolyzed both aliphatic and aromatic acetate esters at substrate concentrations of 0.25 M but did not hydrolyze amino acid esters. Aliphatic alcohols did not inhibit the hydrolysis of p-nitrophenyl acetate; the most potent inhibitors of esterase activity were mercuric chloride, diisopropylfluorophosphate, eserine, and sodium fluoride.

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Mentioned in this Paper

Mercury
TRPC2 gene
Diuron
Structure-Activity Relationship
Isoflurophate
Protoplasm
PON1 gene
PON1
Chromatography, DEAE-Cellulose
Mercuric chloride

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