@article {41144,
	title = {Partial purification and properties of microsomal phosphatidate phosphohydrolase from rat liver.},
	journal = {Biochim Biophys Acta},
	volume = {409},
	year = {1975},
	month = {1975 Nov 21},
	pages = {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.},
	keywords = {Animals, calcium, Deoxycholic Acid, Diglycerides, Hydrogen-Ion Concentration, kinetics, Magnesium, Manganese, Microsomes, Liver, Osmolar Concentration, Phospholipids, Phosphoric Monoester Hydrolases, Rats, Sodium chloride, Structure-Activity Relationship, temperature},
	issn = {0006-3002},
	doi = {10.1016/0005-2760(75)90154-x},
	author = {Caras, I and Shapiro, B}
}
