Add time:09/04/2019         Source:sciencedirect.com

Phosphatidylinositol-specific phospholipase C (PI-PLC) was studied with sonicated dispersions of a thiophosphate analog of phosphatidylinositol, 1,2-dimyristoyloxypropane-3-thiophospho(1d-1-myo-inositol) (d-thio-DMPI). Kinetic parameters were derived from the rate as a function of bulk lipid concentration at constant saturating surface concentration of substrate (case I), and as a function of surface concentration of substrate at a constant saturating bulk concentration of lipid (case II). The substrate, d-thio-DMPI, was diluted with l-thio-DMPI or dimyristoyl phosphatidylmethanol (DMPM). In the presence of l-thio-DMPI, values for Vmax=133 μmol min−1 mg−1, Ks′ (the apparent dissociation constant for the enzyme-interface complex)=0.097 mM, and Km* (the apparent interfacial Michaelis constant)=0.22 mol fraction were obtained. DMPM caused enzyme inhibition in case I but no inhibition in case II. l-Thio-DMPI is an ideal neutral diluent with which to study the kinetics of PI-PLC.

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