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- W2091201813 abstract "The levels of insulin antagonism exhibited by human plasma albumin samples extracted by the alcoholic-trichloroacetic acid (TCA) method were found to vary over a wide range. Similar variations were found in the chlorine contents of these albumin samples, thus indicating a variation in TCA content. Chlorine content correlated with the levels of antagnonism exhibited by the various samples. Both chlorine levels and antagonistic activity were reduced appreciably by chromatography with Dowex 50W ion exchange resin. When Dowex treated (nonantagonistic) albumin was dissolved in water and re-extracted by the TCA-ethanol method, the resulting albumin preparations were high in chlorine content and highly antagonistic toward insulin. Nonantagonistic albumin was rendered antagonistic by the addition of TCA. The levels of antagonism exhibited by the TCA treated albumin preparations correlated with their chlorine contents. It is concluded that at least a portion of the insulin inhibitory effects exhibited by albumin preparations isolated by the TCA-ethanol method is due to TCA which is bound to the protein." @default.
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- W2091201813 date "1973-12-01" @default.
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- W2091201813 title "The nature of the artifactual synalbumin insulin antagonist" @default.
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- W2091201813 doi "https://doi.org/10.1007/bf00461698" @default.
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