[Submergence of Micrococcus lysodeikticus F1-ATPase into the hydrophobic phase of the membrane, using 2,4,6-trinitrobenzosulfonate and 12-0-(azidoformyl) stearic acid methyl ester].
The accessibility of F1-ATPase from Micrococcus lysodeikticus in solution and in the membrane for the specific water-soluble NH2-group reagent, 2,4,6-trinitrobenzosulfonate (TNBS), was studied. Incubation of the soluble factor F1 with 50 mM TNBS pH 8.3 results in incorporation of 58.6 +/- 4.4 trinitrophenyl residues per mole of enzyme. At the same time F1-ATPase isolated from TNBS-pretreated membranes contains 27.2 +/- 2.0 TNP-residues per mole of enzyme. It is assumed that the different accessibility of F1-ATPase for TNBS in solution and in the membrane is due to incorporation of F1-ATPase into the membrane. Study of membrane F1-ATPase interaction with the radioactive lipid-soluble photoreactive label, 12-0-(azidoformyl) stearic acid methyl ester demonstrated that F1-ATPase does not immediately interact with the lipid phase of the membrane. It is suggested that membrane F1-ATPase may be enveloped by hydrophobic proteins.
D000345:Affinity Labels; D001386:Azides; D002462:Cell Membrane / Q000201:enzymology; D007700:Kinetics; D008837:Micrococcus / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D014302:Trinitrobenzenesulfonic Acid
D000345:Affinity Labels; D001386:Azides; C037382:12-O-(azidoformyl)stearic acid methyl ester; D014302:Trinitrobenzenesulfonic Acid; D006180:Proton-Translocating ATPases
Issledovanie pogruzhennosti F1-ATPazy Micrococcus lysodeikticus v gidrofobnuiu fazu membrany s pomoshch'iu 2,4,6-trinitrobenzosul'fonata i metilovogo éfira 12-0-(azidoformil) stearinovoĭ kisloty.