FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2019675781> ?p ?o ?g. }

• W2019675781 endingPage "138" @default.
• W2019675781 startingPage "129" @default.
• W2019675781 abstract "Cytochrome P-448, a type of cytochrome P-450, from brewer's yeast (Saccharomyces cerevisiae) grown under conditions of glucose repression was isolated and purified. Triton X-100 in very low concentration proved to be very effective in stabilizing P-448 in the microsomal fraction and later prevented its conversion to cytochrome P-420 through solubilization with various ionic and nonionic detergents. Highest yields were obtained with 1% sodium cholate, in the presence of 0.1% Triton X-100 and reduced glutathione. A novel combination of hydrophobic adsorption and other chromatographic techniques was used for the purification of cytochrome P-448. These involve the use of amino octyl-Sepharose 4B, instead of the low-yielding aminohexyl derivative, followed by the fast-running hydroxyapatite-cellulose column. Finally, the use of DEAE-Sephacel was found to increase greatly the purity of the cytochrome P-448 obtained. The molecular weight of this preparation was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Mr, 55,500). Using the known molar extinction coefficient of the carbon monoxide-difference spectrum the estimate of degree of purity of cytochrome P-448 obtained by this purification procedure was between 88 and 97%. Electrophoresis also showed that this preparation was completely homogeneous and assays showed that it was also completely free of cytochrome bs, cytochrome c reductase and cytochrome P-420. Purified cytochrome P-448 reconstituted with cytochrome P-450 (cytochrome c) reductase, isolated from yeast, showed 10-fold higher aryl hydrocarbon hydroxylase activity with benzo[a]pyrene as a substrate than the corresponding microsomal fraction enzyme. Kinetics of benzo[a]pyrene hydroxylation were determined: Km (33 μm) was comparable with that reported for purified hepatic cytochrome P-448. The number of binding sites of microsomal and purified cytochromes P-450 (from liver of phenobarbital-induced rats) and yeast cytochrome P-448 with benzo[a]pyrene has been determined using and equilibrium gel filtration method. There is one binding site in each case (contrast with six sites for microsomal enzymes). The Scatchard plot gives number of binding sites, apparent association constants (K), and the equivalent dissociation constants (Ks). Comparison is made with spectral dissociation constants for these enzymes and benzo[a]pyrene. Thus the proportion bound, dissociation constant (Ks), and stoichiometry of rat liver (phenobarbital induced) and yeast cytochrome P-448 with benzo[a]pyrene were compared with corresponding values for microsomal fractions of both systems. Purified enzymes had higher Ks values in both cases, and the proportion of enzyme that bound benzo[a]pyrene was high (53%) for liver and this value is 100% for purified enzyme from yeast, which is the same as the value obtained for the microsomal enzyme from yeast." @default.
• W2019675781 created "2016-06-24" @default.
• W2019675781 creator A5022626440 @default.
• W2019675781 creator A5064242140 @default.
• W2019675781 date "1982-05-01" @default.
• W2019675781 modified "2023-09-27" @default.
• W2019675781 title "Purification and characterization of the cytochrome P-448 component of a benzo(a)pyrene hydroxylase from Saccharomyces cerevisiae" @default.
• W2019675781 cites W1479367516 @default.
• W2019675781 cites W1487793176 @default.
• W2019675781 cites W1490773591 @default.
• W2019675781 cites W1509553808 @default.
• W2019675781 cites W1535984955 @default.
• W2019675781 cites W1594082414 @default.
• W2019675781 cites W1608262032 @default.
• W2019675781 cites W1739192257 @default.
• W2019675781 cites W1775749144 @default.
• W2019675781 cites W1908773839 @default.
• W2019675781 cites W1970608057 @default.
• W2019675781 cites W1971999742 @default.
• W2019675781 cites W1972922373 @default.
• W2019675781 cites W1986974279 @default.
• W2019675781 cites W2003595499 @default.
• W2019675781 cites W2005413144 @default.
• W2019675781 cites W2005528959 @default.
• W2019675781 cites W2012102956 @default.
• W2019675781 cites W2017447305 @default.
• W2019675781 cites W2067776368 @default.
• W2019675781 cites W2069359367 @default.
• W2019675781 cites W2072492018 @default.
• W2019675781 cites W2100837269 @default.
• W2019675781 cites W2414648828 @default.
• W2019675781 cites W2414992988 @default.
• W2019675781 cites W2418907269 @default.
• W2019675781 cites W4318599336 @default.
• W2019675781 doi "https://doi.org/10.1016/0003-2697(82)90261-5" @default.
• W2019675781 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7048997" @default.
• W2019675781 hasPublicationYear "1982" @default.
• W2019675781 type Work @default.
• W2019675781 sameAs 2019675781 @default.
• W2019675781 citedByCount "30" @default.
• W2019675781 countsByYear W20196757812013 @default.
• W2019675781 crossrefType "journal-article" @default.
• W2019675781 hasAuthorship W2019675781A5022626440 @default.
• W2019675781 hasAuthorship W2019675781A5064242140 @default.
• W2019675781 hasConcept C116084860 @default.
• W2019675781 hasConcept C133166286 @default.
• W2019675781 hasConcept C134651460 @default.
• W2019675781 hasConcept C14471203 @default.
• W2019675781 hasConcept C178790620 @default.
• W2019675781 hasConcept C181199279 @default.
• W2019675781 hasConcept C185592680 @default.
• W2019675781 hasConcept C2778913249 @default.
• W2019675781 hasConcept C2778951431 @default.
• W2019675781 hasConcept C2779881004 @default.
• W2019675781 hasConcept C2780768313 @default.
• W2019675781 hasConcept C28859421 @default.
• W2019675781 hasConcept C29311851 @default.
• W2019675781 hasConcept C43617362 @default.
• W2019675781 hasConcept C55493867 @default.
• W2019675781 hasConceptScore W2019675781C116084860 @default.
• W2019675781 hasConceptScore W2019675781C133166286 @default.
• W2019675781 hasConceptScore W2019675781C134651460 @default.
• W2019675781 hasConceptScore W2019675781C14471203 @default.
• W2019675781 hasConceptScore W2019675781C178790620 @default.
• W2019675781 hasConceptScore W2019675781C181199279 @default.
• W2019675781 hasConceptScore W2019675781C185592680 @default.
• W2019675781 hasConceptScore W2019675781C2778913249 @default.
• W2019675781 hasConceptScore W2019675781C2778951431 @default.
• W2019675781 hasConceptScore W2019675781C2779881004 @default.
• W2019675781 hasConceptScore W2019675781C2780768313 @default.
• W2019675781 hasConceptScore W2019675781C28859421 @default.
• W2019675781 hasConceptScore W2019675781C29311851 @default.
• W2019675781 hasConceptScore W2019675781C43617362 @default.
• W2019675781 hasConceptScore W2019675781C55493867 @default.
• W2019675781 hasIssue "1" @default.
• W2019675781 hasLocation W20196757811 @default.
• W2019675781 hasLocation W20196757812 @default.
• W2019675781 hasOpenAccess W2019675781 @default.
• W2019675781 hasPrimaryLocation W20196757811 @default.
• W2019675781 hasRelatedWork W131467418 @default.
• W2019675781 hasRelatedWork W1415782914 @default.
• W2019675781 hasRelatedWork W1963616708 @default.
• W2019675781 hasRelatedWork W2004232103 @default.
• W2019675781 hasRelatedWork W2075759724 @default.
• W2019675781 hasRelatedWork W2075882054 @default.
• W2019675781 hasRelatedWork W2087418933 @default.
• W2019675781 hasRelatedWork W2122673160 @default.
• W2019675781 hasRelatedWork W2403942442 @default.
• W2019675781 hasRelatedWork W94736568 @default.
• W2019675781 hasVolume "122" @default.
• W2019675781 isParatext "false" @default.
• W2019675781 isRetracted "false" @default.
• W2019675781 magId "2019675781" @default.
• W2019675781 workType "article" @default.