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- W2045677079 abstract "The protein and lipid components of Mycoplasma laidlawii membranes disaggregated by sodium dodecyl sulfate (SDS) could not be separated from each other by density-gradient centrifugation, Sephadex-gel filtration, or electrophoresis on cellulose acetate. The addition of sodium deoxycholate (DOC) to SDS for membrane disaggregation enabled the separation of most of the membrane lipid from membrane protein. About 80% of the protein could then be precipitated by ammonium sulfate at 12% saturation and freed of membrane lipids. The precipitated protein was highly hydrophobic and showed a single symmetrical schlieren peak of about 3S when dissolved in SDS. However, disc-gel electrophoresis, under conditions preventing the aggregation of this protein, revealed the presence of more than 10 protein bands. Membrane proteins could also be freed of lipid by 1-butanol extraction. This treatment abolished both the ATPase (EC 3.6.1.3) and NADH2 oxidase (EC 1.6.99.3) activities of the membranes, but disaggregation of the membranes by detergents abolished the ATPase activity only. The relevance of the present findings to the theory that Mycoplasma membranes have a lipoprotein subunit structure is discussed." @default.
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- W2045677079 date "1967-12-01" @default.
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- W2045677079 title "Association of protein and lipid in Mycoplasma laidlawii membranes disaggregated by detergents" @default.
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- W2045677079 doi "https://doi.org/10.1016/0003-9861(67)90168-3" @default.
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