Abstract
Palmityl-CoA: monopalmityl-sn-glycerol 3-phosphate palmitoyltransferase [EC 2.3.1. -] in rabbit mammary gland microsomes is composed of two isoenzymic species. The alpha form (LPAT-alpha) is active with monomeric substrates and inhibited by micelles while the beta form (LPAT-beta) is active only with micelles. By combining the effects of time, temperature, and Tween 80 which selectively inhibited LPAT-alpha, the substrate saturation curve for the LPAT-beta isoenzyme has been successfully determined. Both theoretical and experimental curves are in good agreement.
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