Purification and characterization of chemotactic methylesterase from Bacillus subtilis
- 14 February 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (4) , 675-680
- https://doi.org/10.1021/bi00299a014
Abstract
By utilization of methanol evolution as an assay, a protein methylesterase from B. subtilis was purified. A 1200-fold purification was achieved by CM-Bio-Gel A, hydroxylapatite and Bio-Gel P-60 column chromatography. Gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicate the enzyme is a monomer of 41,000 in MW. The enzyme is stabilized and activated by aqueous glycerol solutions. Methyl-accepting chemotaxis proteins (MCP) serve as substrates for the enzyme. The enzyme requires divalent cation for activity, with maximum activity obtained at 1.1 mM Mg2+. The enzyme is most active at pH 7.5 and at 28.degree. C. Methylesterase has an apprent Km for methylated MCP of .apprx. 10 nM.This publication has 18 references indexed in Scilit:
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