Purification and Characterization of a Novel Plasma Membrane Phosphatidate Phosphohydrolase from Rat Liver
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چکیده
منابع مشابه
Evidence for Histidine Residues on Plasma Membrane Phosphatidate Phosphohydrolase from Rat Liver
Objective(s) Phosphatidate phosphohydrolase (PAP) catalyzes the dephosphorylation of phosphatidic acid to yield Pi and diacylglycerol. Two different forms of PAP in rat hepatocyte have been reported. PAP1 is located in cytosolic and microsomal fractions and participates in the synthesis of triacylglycerols, phosphatidylcholine, and phosphatidylethanolamine, whereas the other form of phosphati...
متن کاملenzymological characteristics of plasma membrane phosphatidate phosphohydrolase (pap2) from rat liver
phosphatidate phosphohydrolase (pap2b, fraction b) was purified from the plasma membrane ofrat liver cells. the km for the surface concentration of phosphatidic acid was 0.43 mol%. the subunit of theenzyme had an m.w. of 33.8 kda using sodium dodecyl sulfate polyacrylamide gel electrophoresis. thenative enzyme shows a molecular weight of 182 kda in a gel filtration column packed with sephacryl ...
متن کاملevidence for histidine residues on plasma membrane phosphatidate phosphohydrolase from rat liver
objective(s) phosphatidate phosphohydrolase (pap) catalyzes the dephosphorylation of phosphatidic acid to yield pi and diacylglycerol. two different forms of pap in rat hepatocyte have been reported. pap1 is located in cytosolic and microsomal fractions and participates in the synthesis of triacylglycerols, phosphatidylcholine, and phosphatidylethanolamine, whereas the other form of phosphatid...
متن کاملPlasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol.
Assays for two distinct phosphatidate phosphohydrolase activities were established based upon a differential inhibition by N-ethylmaleimide (NEM). The activity that is insensitive to this reagent in rat liver is predominantly in the plasma membrane fraction, whereas the NEM-sensitive activity is in the cytosolic and microsomal fractions. The NEM-insensitive activity is further distinguished fro...
متن کاملPurification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects.
A new procedure for the partial purification of Mg2+-dependent, N-ethylmaleimide-sensitive phosphatidate phosphohydrolase (Mg2+-PAP; EC 3.1.3.4) from rat liver cytosol is described, using protein precipitation with MgCl2, gel filtration on Sephacryl S-400, chromatography on DEAE-cellulose and affinity chromatography on calmodulin-agarose. From the parallel change in staining intensity and in th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.33.19422