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- W2079470276 abstract "The hydrophobic interaction chromatography (HIC) of C2C10 acyl coenzyme A (CoA) homologues was investigated in the isocratic mode. Retention of the homologues and of CoA fragments is well described by the empirical salting-out equation, log k′ log k′0 + mMs. Both slope and intercept in this equation increase with carbon number of the homologous series. Simple additivity with carbon number was not found for either slope or intercept. Each additional methylene group had a greater effect on increasing retention than the preceding methylene group. Comparison of the retention of structural fragments of CoA to that of acyl CoA homologues shows that the alkyl moiety of the homologues dominates their retention. The average free energy of transfer of a methylene group from water to a propyl HIC stationary phase was estimated as − 280 cal/mol. The dependence of this free energy of transfer on salt concentration is found to be − 50 cal/mol per 1 M increase in ammonium sulfate concentration." @default.
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- W2079470276 date "1989-01-01" @default.
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- W2079470276 title "Hydrophobic interaction chromatography of small molecules: characterization of the retention of acyl coenzyme a homologues" @default.
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- W2079470276 doi "https://doi.org/10.1016/s0021-9673(01)89634-5" @default.
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