FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1604574498> ?p ?o ?g. }

• W1604574498 endingPage "4417" @default.
• W1604574498 startingPage "4407" @default.
• W1604574498 abstract "Cytochrome P-450scc was isolated from mitochondria of bovine adrenal cortex by hydrophobic chromatography on octyl Sepharose followed by affinity chromatography on cholesterol-7-(thiomethyl)carboxy-3 beta-acetate-Sepharose. The partially purified eluate from the octyl Sepharose resin was free of adrenodoxin and adrenodoxin reductase and displayed biphasic binding characteristics for cholesterol, cholesterol sulfate, and cholesterol acetate (CA). Chromatography of the octyl Sepharose eluate on CA-Sepharose removed extraneous proteins and resolved the cytochrome P-450scc into two fractions, each of which displayed monophasic binding with all three substrates. These fractions behaved identically with respect to their ability to bind substrates, their kinetic properties, and their rate of migration during sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The dissociation constants of the cytochrome P-450scc.substrate complexes are 1.1, 2.6, and 1.3 microM for cholesterol, cholesterol sulfate, and cholesterol acetate, respectively. Addition of phospholipids isolated from adrenal cortex mitochondria or adrenodoxin had no effect on the equilibrium binding constants. Addition of Emulgen 913, however, decreased the binding affinities 10-20-fold. Emulgen 913 also inhibited the interaction of adrenodoxin with the cytochrome. An active side chain cleavage system was reconstituted with purified P-450 by addition of saturating amounts of adrenodoxin, adrenodoxin reductase, and NADPH-generating system. The apparent Km values for this reconstituted system of cholesterol, cholesterol sulfate, and cholesterol acetate are 1.8, 1.9, and 0.6 microM, respectively. Since the Km values of substrate oxidation are similar to the Kd values of the cytochrome P-450.substrate complexes, it seems likely that the binding of substrates, particularly when the side chain cleavage system is free of mitochondrial membranes, is not rate-limiting. Based on these results and electrophoretic data, it appears that one cytochrome P-450 present in adrenal mitochondria can oxidize cholesterol, its sulfate, and its acetate. This enzyme represented about 60% of the cytochrome P-450 present in the octyl Sepharose eluate. The factors responsible for the biphasic kinetics of oxidation by intact mitochondria and biphasic binding of sterol substrates by partially purified preparations of cytochrome P-450scc are still unknown." @default.
• W1604574498 created "2016-06-24" @default.
• W1604574498 creator A5003768870 @default.
• W1604574498 creator A5012502630 @default.
• W1604574498 creator A5041883407 @default.
• W1604574498 creator A5043966723 @default.
• W1604574498 creator A5048521435 @default.
• W1604574498 creator A5058813504 @default.
• W1604574498 date "1981-05-01" @default.
• W1604574498 modified "2023-10-17" @default.
• W1604574498 title "Effects of phospholipid and detergent on the substrate specificity of adrenal cytochrome P-450scc. Substrate binding and kinetics of cholesterol side chain oxidation." @default.
• W1604574498 cites W13356146 @default.
• W1604574498 cites W1482318058 @default.
• W1604574498 cites W1491698474 @default.
• W1604574498 cites W1499670704 @default.
• W1604574498 cites W1526884462 @default.
• W1604574498 cites W1530272666 @default.
• W1604574498 cites W1537954666 @default.
• W1604574498 cites W1556225860 @default.
• W1604574498 cites W1556832027 @default.
• W1604574498 cites W1557487000 @default.
• W1604574498 cites W1566093865 @default.
• W1604574498 cites W1567805507 @default.
• W1604574498 cites W1573792845 @default.
• W1604574498 cites W1628808692 @default.
• W1604574498 cites W1837630174 @default.
• W1604574498 cites W1893933944 @default.
• W1604574498 cites W1951469402 @default.
• W1604574498 cites W1973586477 @default.
• W1604574498 cites W1983649348 @default.
• W1604574498 cites W1985856334 @default.
• W1604574498 cites W1988602702 @default.
• W1604574498 cites W1989300369 @default.
• W1604574498 cites W1990631688 @default.
• W1604574498 cites W1993407080 @default.
• W1604574498 cites W1996696726 @default.
• W1604574498 cites W2000285470 @default.
• W1604574498 cites W2006592781 @default.
• W1604574498 cites W2020823395 @default.
• W1604574498 cites W2037045608 @default.
• W1604574498 cites W2045888839 @default.
• W1604574498 cites W2046491869 @default.
• W1604574498 cites W2050484836 @default.
• W1604574498 cites W2054979333 @default.
• W1604574498 cites W2059836007 @default.
• W1604574498 cites W2061801926 @default.
• W1604574498 cites W2071743090 @default.
• W1604574498 cites W2073325339 @default.
• W1604574498 cites W2075372903 @default.
• W1604574498 cites W2078812370 @default.
• W1604574498 cites W2079938883 @default.
• W1604574498 cites W2080355919 @default.
• W1604574498 cites W2100837269 @default.
• W1604574498 cites W2111301002 @default.
• W1604574498 cites W2168526937 @default.
• W1604574498 cites W2215041997 @default.
• W1604574498 cites W2285897383 @default.
• W1604574498 cites W2321972685 @default.
• W1604574498 cites W255052236 @default.
• W1604574498 cites W4238669140 @default.
• W1604574498 cites W4292477338 @default.
• W1604574498 cites W4293247451 @default.
• W1604574498 cites W63976621 @default.
• W1604574498 cites W98498425 @default.
• W1604574498 doi "https://doi.org/10.1016/s0021-9258(19)69449-4" @default.
• W1604574498 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6260797" @default.
• W1604574498 hasPublicationYear "1981" @default.
• W1604574498 type Work @default.
• W1604574498 sameAs 1604574498 @default.
• W1604574498 citedByCount "27" @default.
• W1604574498 countsByYear W16045744982018 @default.
• W1604574498 countsByYear W16045744982021 @default.
• W1604574498 crossrefType "journal-article" @default.
• W1604574498 hasAuthorship W1604574498A5003768870 @default.
• W1604574498 hasAuthorship W1604574498A5012502630 @default.
• W1604574498 hasAuthorship W1604574498A5041883407 @default.
• W1604574498 hasAuthorship W1604574498A5043966723 @default.
• W1604574498 hasAuthorship W1604574498A5048521435 @default.
• W1604574498 hasAuthorship W1604574498A5058813504 @default.
• W1604574498 hasBestOaLocation W16045744981 @default.
• W1604574498 hasConcept C121332964 @default.
• W1604574498 hasConcept C148898269 @default.
• W1604574498 hasConcept C181199279 @default.
• W1604574498 hasConcept C185592680 @default.
• W1604574498 hasConcept C18903297 @default.
• W1604574498 hasConcept C2777289219 @default.
• W1604574498 hasConcept C2778163477 @default.
• W1604574498 hasConcept C2778918659 @default.
• W1604574498 hasConcept C2780768313 @default.
• W1604574498 hasConcept C28859421 @default.
• W1604574498 hasConcept C29311851 @default.
• W1604574498 hasConcept C2994592520 @default.
• W1604574498 hasConcept C41625074 @default.
• W1604574498 hasConcept C526171541 @default.
• W1604574498 hasConcept C55493867 @default.
• W1604574498 hasConcept C62520636 @default.
• W1604574498 hasConcept C80446465 @default.
• W1604574498 hasConcept C86803240 @default.

• next