The inactivation of rat adipocyte Mg2+-dependent phosphatidate phosphohydrolase by noradrenaline
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چکیده
منابع مشابه
Purification 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...
متن کاملThe effects of Triton X-100 and chlorpromazine on the Mg2+-dependent and Mg2+-independent phosphatidate phosphohydrolase activities of rat lung.
Lung contains both Mg2+-dependent and Mg2+-independent phosphatidate phosphohydrolase activities. Addition of Triton X-100 (0.5%) or chlorpromazine (1 mM) leads to a marked increase in the total phosphatidate phosphohydrolase activity in rat lung microsomes (microsomal fractions), but a decrease in the Mg2+-dependent activity. These observations suggest that the Mg2+-independent activity is sti...
متن کاملTranslocation to rat liver mitochondria of phosphatidate phosphohydrolase.
When a particle-free supernatant fraction from rat liver was incubated at 37 degrees C with mitochondria and oleate, some of the enzyme phosphatidate phosphohydrolase (PAP), initially present in the particle-free supernatant, was recovered, after the incubation, bound to mitochondria. This translocation of PAP from cytosol to mitochondria was stimulated by oleate or palmitate in a similar fashi...
متن کاملStimulation and inhibition of the activity of rat liver cytosolic phosphatidate phosphohydrolase by various phospholipids.
The influence of phospholipids on the activity of the soluble phosphatidate phosphohydrolase from rat liver was studied. Phosphatidylethanolamine stimulated the enzyme activity whereas phosphatidylglycerol, phosphatidylserine, and phosphatidylinositol were inhibitory. At a phospholipid concentration of 0.7 mg/ml, phosphatidylglycerol inhibited phosphatidate phosphohydrolase activity by 75%, whi...
متن کاملTHE EFFECTS OF GLUCAGON, INSULIN AND S TEROID HORMONES ON PHOSPHATIDATE PHOSPHOHYDROLASE ACTIVITY IN RAT LIVERS
The effects of steroid hormones, glucagon and insulin on rat liver phosphatidate phosphohydrolase (PAP) activity were studied both in vitro and in vivo. Incubation of rat hepatocytes with each hormone showed that dehydroepiandrosterone (DHEA), progesterone and testosterone increase PAP activity by 44.6, 37 and 36.9%, respectively. Estradiol, however, decreased enzyme activity by 13.6% under...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1980
ISSN: 0264-6021
DOI: 10.1042/bj1900659