weight, and apparatus dead volume for a solute on a given liquid phase. It is assumed that the isothermal temperature dependence of the retention index is negligible over a range of retention temperatures which might be obtained for different programs. This assumption is valid for the vast majority of solutes, as shown by the data of Kovats (8) and Wehrli and Kovats (IS), who introduced the use of the retention index for isothermal gas chromatography.Retention indices were obtained for some esters, alcohols, aldehydes, and ketones on each of the two columns used under the conditions of this study.

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An investigation is reported of factors affecting the supercritical fluid extraction of sulphamethazine and five of its metabolites from spiked meat (swine liver and kidney). The addition of the polar modifier methanol to the carbon dioxide extracting fluid was found to generally enhance recoveries under subcritical and supercritical conditions. Recoveries of the ionic metabolites were increased by up to 72% when employing tetramethylammonium hydroxide for ion pairing in situ with the supercritical fluid extraction. Extraction efficiency is demonstrated to be dependent on the matrix. Extractions of the less polar compounds from the kidney are more successful than from the liver, which corresponds to their partitioning into the supercritical fluid and/or the greater fraction of highly extractable fatty materials. The kidney was more retentive than liver for the relatively more polar compounds, which suggests that the liver offers a less polar environment under the same extraction conditions.

The interaction of sulphamethazine (SMZ) with pig plasma proteins and albumin was studied by ultrafiltration and equilibrium dialysis. Binding to pig plasma proteins was monophasic (affinity approximately 9.0 mol/L x 10(3)) and the main binding protein was albumin. At 37 degrees C and pH 7.4, the affinity of SMZ for albumin was about 8.0 mol/L x 10(3) and the number of binding sites was estimated as 1.4. Increasing the temperature from 4 to 45 degrees C resulted in a seven-fold decrease in affinity, and increasing pH from 6.0 to 8.0 enhanced affinity for pig albumin ten-fold. The free energy of binding (-delta G) and enthalpy change (-delta H) were around 5.5 and 5.1 Kcal/mol, respectively. The total entropy change (delta S) was small and positive, around 2 cal/mol/degree K. Studies with the fluorescent probes warfarin and dansylsarcosine, suggest that these bind to separate sites on porcine albumin. SMZ displaced both probes and inhibited the deacetylation of p-nitrophenyl acetate by pig albumin. We conclude that: (1) binding of SMZ to pig plasma proteins and albumin is weak; (2) the interaction with albumin is exothermic and enthalpy driven, and (3) pig albumin, like other mammalian albumins, appears to possess discrete binding sites for warfarin and dansylsarcosine. SMZ interacts with both these loci.