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- W2016158575 abstract "Abstract The nature of the linkage between phosphatidopeptides and residual protein and the linkage between phosphoinositide and protein in phosphatidopeptides from beef-brain white matter have been investigated by using various modifications in the extraction procedure. It was found that the phosphoinositide can be almost completely dissociated from all protein by using a sufficiently non-polar acidified solvent for the extraction. When more polar solvents are used increasing amounts of protein are obtained in the extracts, a substantial amount of which is bound to the extracted phosphoinositide. The data are consistent with the hypothesis that this extractable phosphoinositide-protein complex exists in situ and is not an artifact of preparation. In solvents of relatively high polarity the extracts also include some protein which is soluble by itself in the organic solvents. The principal type of bonding in both sites involved in the phosphatidopeptides appears to be electrostatic. Chemical analyses of the various extracts showed that the major lipid constituent in all cases was probably triphosphoinositide with negligible contamination by phosphatides which do not contain inositol. The variations in amino acids and other N constituents were also established." @default.
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- W2016158575 date "1963-01-01" @default.
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- W2016158575 title "The nature of the linkage between phosphoinositides and proteins in brain" @default.
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- W2016158575 doi "https://doi.org/10.1016/0006-3002(63)90810-2" @default.
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