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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.