The effect of the incorporation of linear (perfluoroalkyl)alkanes (CmF2m + 1CnH2n + 1, FmHn) into liposomes made of DMPC or DPPC on the activity of porcine pancreatic phospholipase A2 was investigated. A large decrease in enzyme activity and modifications of the kinetic profile, especially at and above the phospholipid's phase transition temperature, were observed; both depend on the relative lengths of the phospholipid's fatty acid chains and of the Hn segment of the FmHn molecule. With DMPC Hn must have a minimum of 10 carbon atoms to be effective, as in F6H10, F8H10 and F4H12; F8H8 had no significant hydrolysis-rate-reducing effect.
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May 1992
Branchial activities of Na(+),K(+)-ATPase (ouabain sensitive), Mg(2+) ATPase (ouabain insensitive) and kinetic analysis of high and low affinity Ca(2+) ATPase were measured inAnguilla anguilla that had been acclimated to demineralized water (DW, Ca < 10 μM), freshwater (FW, Ca = 2 mM), and Low calcium freshwater (L-Ca, Ca = 0.9 mM). Na(+),K(+)-ATPase activity decreased while ouabain insensitive activity increased when ambient Ca(2+) decreased.
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