[Characteristics of subunit composition of H+-ATPase from the anaerobic bacterium Lactobacillus casei].
In the presence of Mg2+ or Ca2+ the membranes of the anaerobic glycolytic bacterium Lactobacillus casei hydrolyze 0.1-0.2 mumole ATP/min/mg of protein with a pH optimum 6.4. This activity is inhibited by N,N'-dicyclohexylcarbodiimide and is insensitive to oligomycin, ouabain, vanadate and hydroxylamine. A soluble ATPase was isolated and purified from L. casei membranes. The specific activity of this ATPase is 3.0-4.0 mumole ATP/min/mg of protein. The enzyme homogeneity was established by analytical polyacrylamide gel disc electrophoresis and by analytical centrifugation (S20, omega = 12 +/- 0,5). The molecular weight of the enzyme is 270 000. Polyacrylamide gel electrophoresis of ATPase denaturated by 1% SDS and 8 M urea in the presence of SDS revealed one type of subunits with Mr = 43 000. These subunits could not be separated by isoelectrofocusing in polyacrylamide gel in the presence of 8 M urea and migrated as a single peptide with pI at 4.2. The experimental results suggest that the soluble ATPase from L. casei consists of six identical subunits with Mr of 43 000.
D000693:Anaerobiosis; D002118:Calcium / Q000494:pharmacology; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D006180:Proton-Translocating ATPases / Q000302:isolation & purification* / Q000378:metabolism
D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases; D008274:Magnesium; D002118:Calcium
Osobennosti sub''edinichnogo sostava H+-ATPazy iz anaérobnoĭ bakterii Lactobacillus casei.