Abstract
The cytoplasmic membrane of Mycoplasma laidlawii strain B is solubilized by anionic and nonionic detergents, succinylation, phospholipase A, alkaline phosphatase, trypsin, and chymotrypsin. Cationic detergents are without effect, as are chelating agents, even in the presence of high concentrations of monovalent cation. The detergent-solubilized membrane exhibits one peak in the analytical ultracentrifuge, but the sedimentation coefficient is dependent upon concentration of detergent. Simple dialysis does not remove all of the sodium dodecylsulfate except from lipid-depleted membrane particles. Membranes bind sodium dodecylsulfate but acetone powders of membranes do not. Sulfated alcohols with chain lengths of C(14) and C(16) are more tightly bound than dodecylsulfate. A constant amount of di- and trivalent cation is bound by the membrane upon aggregation. Only a portion of this cation is removable with chelating agents. No chelating agent is bound by these aggregates. A portion of the lipid-depleted membrane particles is solubilized by negatively charged lipids and detergents, giving rise to aggregates in the presence of divalent cation. Fractionations of detergent-solubilized membranes by preparative gel electrophoresis and ammonium sulfate were inconclusive. Density gradient centrifugation of succinylated membranes yielded at least five fractions which exhibited homogeneity by ultracentrifugation. Analytical gel electrophoresis of these fractions demonstrated heterogeneity. The composition of these five fractions suggested separation of protein from lipid.