[Proteins of bacterial membranes. Purification of soluble ATPase from Acholeplasma laidlawii].
A purified preparation of ATPase (factor F1) from the Acholeplasma laidlawii was obtained. The purification procedure included extraction of the enzyme complex from the isolated membranes by ultrasonication, chromatography on DEAE-cellulose and gel filtration on Sepharose 6B. The specific activity of the ATPase was increased 30-fold as compared to the original activity. The Km value for ATP hydrolysis was 7,4 . 10(-4) M. ADP competitively inhibited the enzyme (Ki = 2,0 . 10(-4) M). Ouabain (2,5 . 10(-4) M) and dicyclohexylcarbodiimide (1,0 . 10(-4) M) did not inhibit the ATPase activity. The enzyme was activated by Mg2+, but was inhibited by a combination of Na+ and K+. The enzyme is cold-labile, but can be stabilized by storage in buffer solutions, containing methanol, glycerol or lecithin.
D000128:Acholeplasma laidlawii / Q000201:enzymology*; D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D012964:Sodium / Q000494:pharmacology
D004024:Dicyclohexylcarbodiimide; D010042:Ouabain; D012964:Sodium; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium
Belki bakterial'nykh membran. Ochistka vodorastvorimoĭ ATPazy iz Acholeplasma laidlawii.