PMID: 9555Aug 1, 1976

Interactions of phospholipase D with 1,2 diacyl-sn-glycerol-3-phosphorylcholine, dodecylsulfate, and Ca2+

M HellerI Peri


Some properties of the pure, soluble phospholipase D (phosphatidycholine phosphatido hydrolase, EC interactions with phosphatidyl choline (1,2 diacyl-sn-glycerol-3-phosphoryl choline) in a system also containing dodecylsulfate and Ca2+ ions were studied. Concentrations of Ca2+ greater than 50 mM were necessary both for activity and adsorption of the enzyme to the "supersubstrate." Ethylenediamine tetraacetic acid caused inhibition of activity, greater than one would expect from its chelating capacity. A nonlinear increase in activity with the increase of enzyme protein was observed, suggesting a subunit aggregation into a higher mol wt protein, catalytically more active. Upon centrifugation of the supersubstrate-enzyme complex at 4.5 X 10(5) g-min at 30 C, most of the substrate molecules sedimented regardless of the pH. The reverse was true when centrifugation was done at 1 C. Phospholipase D hydrolyzed phosphatidylcholine molecules present in the supersubstrate at temperatures around 0 C at a rate 1/5 that of a maximal value measured at 30 C. The Arrhenius plot was linear in the range from 0 to 30 C, and at that temperature the curve broke with a smaller slope. Activation energy of 9.1 Kcal/mol, below 30 C, was calcul...Continue Reading


Oct 5, 1972·Biochimica Et Biophysica Acta·R Tzur, B Shapiro
Jan 1, 1968·Progress in Biophysics and Molecular Biology·A D BANGHAM
Jan 6, 1970·Biochimica Et Biophysica Acta·M C PhillipsD Chapman
Jul 14, 1970·Biochimica Et Biophysica Acta·M Heller, R Arad


Apr 1, 1978·Journal of the American Oil Chemists' Society·R G JensenK E McMahon
May 23, 1998·Biochimica Et Biophysica Acta·N DittrichR Ulbrich-Hofmann
Oct 24, 2008·Chembiochem : a European Journal of Chemical Biology·Konstantin KuppeR Ulbrich-Hofmann

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