Properties of phosphatidate phosphohydrolase in rat adipose tissue
نویسندگان
چکیده
منابع مشابه
Translocation 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 کاملGlycerolipid synthesis in rat adipose tissue. II. Properties and distribution of phosphatidate phosphatase.
The properties and subcellular distribution of phosphatidate phosphatase (EC 3.1.3.4) from adipose tissue have been investigated. The enzyme was assayed using both aqueous phosphatidate and membrane-bound phosphatidate as substrates. When measured with aqueous substrate, activity was detected in the mitochondria, the microsomes, and the soluble fraction. Mg(2+) at low concentration stimulated t...
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...
متن کاملAdipose-tissue Mg2+-dependent phosphatidate phosphohydrolase. Control of activity and subcellular distribution in vitro and in vivo.
The subcellular distribution of Mg2+-dependent phosphatidate phosphohydrolase in rat adipocytes between a soluble and a membrane-bound fraction was measured by using both centrifugal fractionation and a novel Millipore-filtration method. The relative proportion of the phosphohydrolase associated with the particulate fraction was increased on incubation of cells with noradrenaline or palmitate. ...
متن کاملA rapid sensitive assay for phosphatidate phosphohydrolase.
For a purified preparation of the soluble form of phosphatidate phosphohydrolase (EC 3.1.3.4) from guinea pig cerebral cortex, I-O-alkyl-racglycerol 3-phosphate was found to be accepted as a substrate. This substrate analog was tritium-labeled in order to serve in a rapid sensitive assay for the enzyme, in which labeled I-alkyl glycerol is released. Heat denaturation and enzyme activity depende...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3010793