[Comparative study of different variants of Actinomyces roseoflavus producing the polyene antibiotic roseofungin]. / Sravnitel'noe issledovanie razlichnykh variantov Actinomyces roseoflavus, obrazuiushchego polienovyi antibiotik rozeofungin.

The respiration chain in the membranes of whole Actinomyces roseoflavus (var. roseofungini) cells from the parent and secondary cultures is sensitive to KCN, non-sensitive to Triton X-100 treatment removing the antibiotic roseofungin from the cells, and has a very high for the bacteria respiration control. When the cells are in contact with atomic tritium at the temperature of liquid nitrogen, roseofungin is tritiated and binds to A. roseoflavus isolated membranes and whole cells, mostly to those of the parent culture as compared to the secondary culture. A fraction of membranes which lost NADH dehydrogenase in the course++ of purification was isolated from the cells disintegrated in the frozen state.

[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]. / Issledovanie pogruzhennosti F1-ATPazy Micrococcus lysodeikticus v gidrofobnuiu fazu membrany s pomoshch'iu 2,4,6-trinitrobenzosul'fonata i metilovogo éfira 12-0-(azidoformil) stearinovoi kisloty.

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.