Publications

1975
I Caras and B Shapiro. 1975. “Partial purification and properties of microsomal phosphatidate phosphohydrolase from rat liver.” Biochim Biophys Acta, 409, 2, Pp. 201-11.Abstract
Microsomal phosphatidate phosphohydrolase (phosphatidate phosphatase EC 3.1.3.4) was solubilized and fractionated to yield at least two distinct enzymatically active fractions. One, denoted FA, was non-specific, had a relatively high Km for phosphatidic acid and was insensitive to inhibition by diacylglycerol. The second fraction, FB, was specific for phosphatidates, had a low Km, and was inhibited, non-competitively, by diacylglycerol. FA exhibited a sigmoid substrate-activity curve. The isolated FB aggregated to particles of about 10(6) in the absence of salts and could be dissociated by the addition of monovalent cations at ionic strength 0.4-0.6 to about 2-10(5) daltons and thereby doubled its activity. Dissociation was time- and temperature-dependent. F- was inhibitory. Divalent ions were not required for the activity of FA or FB and inhibited at concentrations exceeding 1 mM.
D Osborn and DH Jenkinson. 1975. “Proceedings: Comparison of the effects of selective alpha and beta-receptor agonists on intracellular cyclic AMP levels and glycogen phosphorylase activity in guinea-pig liver.” Br J Pharmacol, 55, 2, Pp. 286P-287P.
J Marniemi and MG Parkki. 1975. “Radiochemical assay of glutathione S-epoxide transferase and its enhancement by phenobarbital in rat liver in vivo.” Biochem Pharmacol, 24, 17, Pp. 1569-72.
YW Chow, R Pietranico, and A Mukerji. 1975. “Studies of oxygen binding energy to hemoglobin molecule.” Biochem Biophys Res Commun, 66, 4, Pp. 1424-31.

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