Matches in SemOpenAlex for { <https://semopenalex.org/work/W602657775> ?p ?o ?g. }
Showing items 1 to 63 of
63
with 100 items per page.
- W602657775 abstract "approved: Redacted for privacy Dr. Donald R. Buhler Utilizing new techniques for solubilization and initial purification, cytochromes P-450 and NADPH-cytochrome P-450 reductase were purified from liver microsomes of 8-naphthoflavone-treated rainbow trout. The properties of the trout enzymes were compared to rat cytochromes P-450 and P-448 and NADPH-cytochrome P-450 reductase using a number of criteria for distinguishing multiple isozyme forms. A minimum of four to five cytochrome P-450 forms were purified from -naphthoflavone-treated trout. The major form was similar to cytochrome P-448 from f3-naphthoflavone-treated rat with respect to spectral properties, activity and regioselectivity towards benzo(a)PYrene, and sensitivity to in vitro inhibitors. However, rat and trout cytochrome P-448 differed in substrate specificity, molecular weight and did not share identical antigenic determinants. Rat and trout cytochrome P-448 were quite different from P-450 from phenobarbital-treated rats using all of the above criteria for distinguishing multiple forms. A single form of NADPH-cytochrome P-450 reductase was also purified from 8-naphthoflavone-treated rainbow trout. Comparison with NADPH-cytochrome P-450 reductase purified from phenobarbitaltreated rat, showed that the two enzymes differed markedly in spectral properties, molecular weight, amino acid and flavin composition and peptide profiles following limited proteolysis. Cytochrome c reduction by the trout enzyme was inhibited by antibody to rat NADPHcytochrome P-450 reductase, but not to the same extent as was the rat enzyme. No precipitin lines between trout NADPH-cytochrome P-450 reductase and rat antibody were observed on Ouchterlony plates. Comparison of ethoxyresorufin-O-deethylase temperature profiles with various combinations of trout and rat cytochrome P-448, NADPHcytochrome P-450 reductase and lipid, in membranous and non-membranous reconstitution systems, demonstrated that the lower temperature optimum of trout microsomes could only be reproduced when all three trout components were incorporated into liposomes. These results suggest that it is the structural organization of the mixed-function oxidase enzymes and lipid within trout microsomes which are responsible for the lower temperature optimum compared to mammalian mixedfunction oxidase reactions. PURIFICATION, CHARACTERIZATION AND COMPARATIVE PROPERTIES OF HEPATIC MICROSOMAL MIXED-FUNCTION OXIDASE ENZYMES FROM RAT AND RAINBOW TROUT by David Edward Williams" @default.
- W602657775 created "2016-06-24" @default.
- W602657775 creator A5053837229 @default.
- W602657775 date "1982-11-11" @default.
- W602657775 modified "2023-09-24" @default.
- W602657775 title "Purification, characterization and comparative properties of hepatic microsomal mixed-function oxidase enzymes from rat and rainbow trout" @default.
- W602657775 hasPublicationYear "1982" @default.
- W602657775 type Work @default.
- W602657775 sameAs 602657775 @default.
- W602657775 citedByCount "0" @default.
- W602657775 crossrefType "dissertation" @default.
- W602657775 hasAuthorship W602657775A5053837229 @default.
- W602657775 hasConcept C134651460 @default.
- W602657775 hasConcept C153911025 @default.
- W602657775 hasConcept C181199279 @default.
- W602657775 hasConcept C185592680 @default.
- W602657775 hasConcept C2779363728 @default.
- W602657775 hasConcept C2780768313 @default.
- W602657775 hasConcept C2909208804 @default.
- W602657775 hasConcept C2994167347 @default.
- W602657775 hasConcept C505870484 @default.
- W602657775 hasConcept C55493867 @default.
- W602657775 hasConcept C86803240 @default.
- W602657775 hasConcept C87644729 @default.
- W602657775 hasConceptScore W602657775C134651460 @default.
- W602657775 hasConceptScore W602657775C153911025 @default.
- W602657775 hasConceptScore W602657775C181199279 @default.
- W602657775 hasConceptScore W602657775C185592680 @default.
- W602657775 hasConceptScore W602657775C2779363728 @default.
- W602657775 hasConceptScore W602657775C2780768313 @default.
- W602657775 hasConceptScore W602657775C2909208804 @default.
- W602657775 hasConceptScore W602657775C2994167347 @default.
- W602657775 hasConceptScore W602657775C505870484 @default.
- W602657775 hasConceptScore W602657775C55493867 @default.
- W602657775 hasConceptScore W602657775C86803240 @default.
- W602657775 hasConceptScore W602657775C87644729 @default.
- W602657775 hasLocation W6026577751 @default.
- W602657775 hasOpenAccess W602657775 @default.
- W602657775 hasPrimaryLocation W6026577751 @default.
- W602657775 hasRelatedWork W1490773591 @default.
- W602657775 hasRelatedWork W1969083764 @default.
- W602657775 hasRelatedWork W1986889504 @default.
- W602657775 hasRelatedWork W2001045378 @default.
- W602657775 hasRelatedWork W2014398730 @default.
- W602657775 hasRelatedWork W20207240 @default.
- W602657775 hasRelatedWork W2027388361 @default.
- W602657775 hasRelatedWork W2035363866 @default.
- W602657775 hasRelatedWork W2049240148 @default.
- W602657775 hasRelatedWork W2051445339 @default.
- W602657775 hasRelatedWork W2055143767 @default.
- W602657775 hasRelatedWork W2086574994 @default.
- W602657775 hasRelatedWork W2088612995 @default.
- W602657775 hasRelatedWork W2339240598 @default.
- W602657775 hasRelatedWork W2412751402 @default.
- W602657775 hasRelatedWork W2443225115 @default.
- W602657775 hasRelatedWork W2481713884 @default.
- W602657775 hasRelatedWork W2485202966 @default.
- W602657775 hasRelatedWork W2922451867 @default.
- W602657775 hasRelatedWork W3213421860 @default.
- W602657775 isParatext "false" @default.
- W602657775 isRetracted "false" @default.
- W602657775 magId "602657775" @default.
- W602657775 workType "dissertation" @default.