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Characterization of a K+-ATPase from Lactobacillus helveticus ATCC 15009



Characterization of a K+-ATPase from Lactobacillus helveticus ATCC 15009



Archives of Microbiology 168(3): 205-209



Lactobacillus helveticus ATCC 15009 (wild-type) membrane preparations hydrolyzed Mg-2+-ATP as a function of K+ concentration (2-200 mM). Mg-2+-ATP hydrolysis by L. helveticus membranes was strongly inhibited in the absence of exogenous K+, while it amounted to 6 nmol ATP hydrolyzed min-1 (mg membrane protein)-1 at 50 mM KCl (saturating conditions) and pH 7.2. The K+-dependent ATPase of L. helveticus displayed a relatively high affinity for potassium ions (K-m = 800 mu-M) and was not affected by pretreatment of membranes with N,N'-dicyclohexylcarbodiimide. Membrane preparations were subjected to hypotonic shock to obtain a maximum yield of open profiles. The formation of a maximum level of enzyme-phosphate complex with a molecular mass of approximately 82 kDa was induced upon treatment of L. helveticus membrane preparations with low concentrations of (gamma-32P)ATP in the presence of K+ and La-3+ ions and was visualized by acidic SDS-PAGE. It was concluded that L. helveticus membranes contain an inwardly directed K+ pump whose presence is discussed in terms of its putative role in cytoplasmic pH regulation.

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Accession: 002775293

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DOI: 10.1007/s002030050489


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