Studies on the ATPase of  Bacillus cereus | Zendy

Higuti I. H. | Zendy; Stencel M. | Zendy; Nascimento K. H. | Zendy; Nascimento A. J. | Zendy

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Studies on the ATPase of Bacillus cereus

Author(s) -

Higuti I. H.,

Stencel M.,

Nascimento K. H.,

Nascimento A. J.

Publication year - 1992

Publication title -

cell biochemistry and function

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.933

H-Index - 61

eISSN - 1099-0844

pISSN - 0263-6484

DOI - 10.1002/cbf.290100405

Subject(s) - bacillus cereus , chemistry , chromatography , enzyme , atpase , biochemistry , polyacrylamide gel electrophoresis , centrifugation , electrophoresis , divalent , gel electrophoresis , glycerol , molecular mass , biology , bacteria , genetics , organic chemistry

The membrane ATPase (EC 3.6.1.3) of Bacillus cereus was solubilized by a ‘shock‐wash’ process and purified. The non‐specific phosphatase contaminant was separated by glycerol density gradient centrifugation. The optimum temperature was 39·5°C and the pH optimum at 7·5. On SDS‐polyacrylamide gel electrophoresis two classes of subunits were observed in equal proportions with molecular weights of 70 K and 83 K. The effect of various compounds on the enzymatic activity was studied. The enzyme was insensitive to NaN 3 , oligomycin and to divalent cations, but was inhibited by citrate and oxalate.

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