Sterol carrier protein2-like activity in rat intestine.
نویسندگان
چکیده
منابع مشابه
The participation of sterol carrier protein2 in the conversion of cholesterol to cholesterol ester by rat liver microsomes.
The purification of sterol carrier protein2 (SCP2), purified 1500-fold to homogeneity from the 303,000 x g supernatant (S303) of rat liver, has recently been described (Noland, B. J., Arebalo, R. E., Hansbury, E., and Scallen T. J. (1980) J. Biol. Chem, 255, 4282-4289). Since SCP2 is required for the synthesis of cholesterol by microsomal membranes, it was decided to test the hypothesis that SC...
متن کاملSterol carrier protein2. Delivery of cholesterol from adrenal lipid droplets to mitochondria for pregnenolone synthesis.
The ability of sterol carrier protein2 (SCP2) to mediate transfer of unesterified cholesterol from adrenal lipid inclusion droplets to mitochondria has been tested in an in vitro model system. Unlike mitochondrial utilization of cholesterol added in acetone or dimethyl sulfoxide, the unesterified cholesterol of lipid droplets did not provide a readily available source of substrate for mitochond...
متن کاملStudies on the Synthesis of Sterol Carrier Protein-2 in Rat Adrenocortical Cells in Monolayer Culture
The effects of ACTH or dibutyryl cyclic AMP (Bt2 CAMP) on the synthesis of sterol carrier protein-2 (SCP2) have been studied in rat adrenocortical cells in monolayer culture. Radiolabeling of total cellular proteins with [3SS]methionine and immunoprecipitation with antibodies directed against rat liver SCP2, followed by polyacrylamide gel electrophoresis and fluorography, showed a 3-4-fold incr...
متن کاملSubcellular localization of sterol carrier protein-2 in rat hepatocytes: its primary localization to peroxisomes
Sterol carrier protein-2 (SCP-2) is a nonenzymatic protein of 13.5 kD which has been shown in in vitro experiments to be required for several stages in cholesterol utilization and biosynthesis. The subcellular localization of SCP-2 has not been definitively established. Using affinity-purified rabbit polyclonal antibodies against electrophoretically pure SCP-2 from rat liver, we demonstrate by ...
متن کاملPurification and properties of sterol carrier protein1.
Previous studies have demonstrated that both the 105,000 X g soluble supernatant (S105) and microsomal membranes from rat liver are required for the enzymatic conversion of squalene to cholesterol (Scallen, T.J., Dean, W.J., and Schuster, M.W. (1968) J. Biol. Chem. 243, 5202). It was postulated that S105 contained a noncatalytic carrier protein which was required for this enzymatic process (Sca...
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ژورنال
عنوان ژورنال: Journal of Lipid Research
سال: 1988
ISSN: 0022-2275
DOI: 10.1016/s0022-2275(20)38535-7