PMID: 64Nov 21, 1975

Partial purification and properties of microsomal phosphatidate phosphohydrolase from rat liver

Biochimica Et Biophysica Acta
I Caras, B Shapiro


Microsomal phosphatidate phosphohydrolase (phosphatidate phosphatase EC 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.


Aug 31, 1987·Clinica Chimica Acta; International Journal of Clinical Chemistry·K SumikawaH Nishimura
Feb 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·B J Benson
Oct 1, 1978·Acta Physiologica Scandinavica·V L KinnulaI Hassinen
Jun 15, 1978·Analytical Biochemistry·J E BleasdaleB W Agranoff
May 15, 1986·Analytical Biochemistry·R K KellerN Cafmeyer
Apr 6, 2000·The Journal of Eukaryotic Microbiology·C Tellis, M E Lekka
Nov 1, 1989·Journal of Neuroscience Research·K K Vaswani, R W Ledeen
Apr 1, 1978·European Journal of Biochemistry·H Kanoh, B Akesson
Apr 15, 1976·European Journal of Biochemistry·R Tzur, B Shapiro

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Deoxycholic Acid, Monoammonium Salt
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