Binding of Triton X-100 to purified cytochrome P-450scc and enhancement of the cholesterol side chain cleavage activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. Cytochrome P-450 from Bovine Adrenocortical Mitochondria: an Enzyme for the Side Chain Cleavage of Cholesterol
2. Cytochrome P-450 from Bovine Adrenocortical Mitochondria: an Enzyme for the Side Chain Cleavage of Cholesterol
3. Stereochemical specificity at carbon-20 and -22 of hydroxylated cholesterols for side-chain cleavage by adrenocortical cytochrome P -450scc
4. The enzyme activity of bovine adrenocortical cytochrome P-450 producing pregnenolone from cholesterol: Kinetic and electrophoretic studies on the reactivity of hydroxycholesterol intermediates
5. A procedure for the estimation of microgram quantities of Triton X-100
Cited by 14 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. A Central Role for Water in the Control of the Spin State of Cytochrome P-450scc;European Journal of Biochemistry;1997-12
2. Cholesterol monooxygenase (side-chain-cleaving);Enzyme Handbook;1994
3. Cytochrome P-450scc-substrate interactions. Role of the 3 beta- and side chain hydroxyls in binding to oxidized and reduced forms of the enzyme.;Journal of Biological Chemistry;1986-02
4. Cytochrome P-450 Organization and Membrane Interactions;Cytochrome P-450;1986
5. The biosynthesis of triterpenoids and steroids;Natural Product Reports;1985
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