Molecular Cloning and Expression of Rat Squalene Epoxidase
نویسندگان
چکیده
منابع مشابه
Squalene Epoxidase of Rat Liver*
The microsomal enzyme system from rat liver which catalyzes the epoxidation of squalene to 2,3-oxidosqualene (squalene epoxidase) has been investigated further with 10 ,ll-dihydrosqualene as the artacial substrate. Liver supernatant contributes two essential components to the epoxidase system, one heat stable and the other heat labile (YAMAMOTO, S., AND BLOCH, K. (1970) J. Biol. Chem. 245, 1670...
متن کاملStudies on Squalene Epoxidase of Rat Liver*
Rat liver microsomes previously heated to 50” for 5 mm accumulate 2,3-oxidosqualene on incubation with squalene. Squalene epoxidase activity can be assayed either with squalene and heated microsomes or with lO,ll-dihydrosqualene and intact microsomes. In common with other monooxygenases, the epoxidase requires TPNH and molecular oxygen. Both a soluble fraction of rat liver and microsomes are ne...
متن کاملStudies on squalene epoxidase of rat liver.
Rat liver microsomes previously heated to 50” for 5 mm accumulate 2,3-oxidosqualene on incubation with squalene. Squalene epoxidase activity can be assayed either with squalene and heated microsomes or with lO,ll-dihydrosqualene and intact microsomes. In common with other monooxygenases, the epoxidase requires TPNH and molecular oxygen. Both a soluble fraction of rat liver and microsomes are ne...
متن کاملRegulation of squalene epoxidase activity in rat liver.
Regulation of squalene epoxidase activity was examined in rat hepatic microsomes. The hepatic squalene epoxidase activity was high in the dark period and low in the light period. Three percent cholestyramine feeding increased the hepatic squalene epoxidase activity by 2.5-fold, and the administration of lovastatin, an inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, incre...
متن کاملPurification and characterization of recombinant squalene epoxidase.
Recombinant rat squalene epoxidase (rSE) was expressed in E. coli and purified to an apparent homogeneity. This expression system was constructed using squalene epoxidase (SE) cDNA in which nucleotides coding 99 amino acids in the N-terminal were deleted and nucleotides coding hexa-histidine in the C-terminal were added. Purification was carried out using Ni-chelate affinity agarose and Cibacro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.1.17