[Evidence for the presence of H+-ATPase in the membrane of brain synaptic vesicles in the rat].
Mg-ATPase of rat brain synaptic vesicles (SV) is considerably (by 85%) inhibited by dicyclohexyl carbodiimide (200 microM), a blocker of proton pumps, whereas orthovanadate (100 microM) does not produce any influence on the enzyme. Oligomycin (5 micrograms/ml) does not alter Mg-ATPase activity of the SV, whereas N-ethylmaleimide (300 microM) reduces it to a moderate degree, namely by 35%. This indicates that Mg-ATPase of the SV differs from mitochondrial ATPase. The protonophore p-trichloromethoxycarbonyl cyanide phenylhydrazone (20 microM) and bicarbonate anions (20 mM) stimulate slightly (by 12 to 25%) Mg-ATPase of the SV. Bicarbonate (20 mM) raises 1.8-2.1-fold Mg-ATPase activity of the mitochondria isolated from rat brain. It is assumed that the membrane of brain SV contains proton ATPase (H+-ATPase) differing from mitochondrial H+-ATPase in some of the properties.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology*; D017301:Ca(2+) Mg(2+)-ATPase; D008565:Membrane Proteins / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011522:Protons; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D013572:Synaptic Vesicles / Q000201:enzymology*
D008565:Membrane Proteins; D011522:Protons; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D006180:Proton-Translocating ATPases; D000254:Sodium-Potassium-Exchanging ATPase
Dokazatel'stva nalichiia H+-ATFazy v membrane sinapticheskikh puzyr'kov mozga krys.