Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-11-9
pubmed:abstractText
Cytochromes P450 beta NF-A, beta NF-B, and beta NF-C were purified from beta-naphthoflavone-treated adult hens. Cytochrome P450 beta NF-A, however, appeared at two places in the purification scheme. They were designated as cytochromes P450 beta NF-A1 and beta NF-A2 for property comparison. The cytochromes beta NF-A1 and beta NF-A2 were induced by both phenobarbital and beta-naphthoflavone treatment and were similar to P450 PB-A (previously purified from phenobarbital-induced hen livers) in molecular weights, isoelectric pH, spectral properties, behavior on chromatography columns, catalysis of substrates, immunological cross-reactivity on Ouchterlony plates and by immunoblotting, and NH2-terminal amino acid sequence. However, P450 PB-A differed from beta NF-A1/beta NF-A2 in peptide pattern after partial proteolysis by alpha-chymotrypsin and Staphylococcus aureus V8 protease, and complete digestion of 125I-labeled cytochromes by trypsin. The cytochrome P450 PB-A also differed from beta NF-A1/beta NF-A2, in that its antibodies cross-reacted with P-450 of normal, PB-, and beta-NF-induced rabbit liver microsomes. The cytochromes beta NF-B and beta NF-C, although immunochemically cross-reactive with each other, were distinct enzymes on the basis of molecular weights, spectral characteristics, isoelectric pH, peptide pattern on partial proteolysis, tryptic peptide pattern, cross-reactivity of their antibodies with other species, and NH2-terminal amino acid sequence. The most notable difference between beta NF-B and beta NF-C was that the anti-beta NF-C IgG completely inhibited O-dealkylation of 7-methoxyresorufin and 7-ethoxyresorufin by beta-NF-induced microsomes. These activities increased 40- to 50-fold in beta-NF-induced microsomes as compared to only 2- to 4-fold in PB-treated hens. The amino-terminal sequences of beta NF-B and beta NF-C were different from those of mammalian and other nonmammalian species.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
170-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2171427-Amino Acid Sequence, pubmed-meshheading:2171427-Animals, pubmed-meshheading:2171427-Benzoflavones, pubmed-meshheading:2171427-Chickens, pubmed-meshheading:2171427-Chromatography, pubmed-meshheading:2171427-Chromatography, Affinity, pubmed-meshheading:2171427-Chromatography, DEAE-Cellulose, pubmed-meshheading:2171427-Chromatography, Ion Exchange, pubmed-meshheading:2171427-Cytochrome P-450 Enzyme System, pubmed-meshheading:2171427-Cytochromes b5, pubmed-meshheading:2171427-Durapatite, pubmed-meshheading:2171427-Enzyme Induction, pubmed-meshheading:2171427-Female, pubmed-meshheading:2171427-Hydroxyapatites, pubmed-meshheading:2171427-Isoenzymes, pubmed-meshheading:2171427-Microsomes, Liver, pubmed-meshheading:2171427-Molecular Sequence Data, pubmed-meshheading:2171427-Molecular Weight, pubmed-meshheading:2171427-Peptide Fragments, pubmed-meshheading:2171427-Phenobarbital, pubmed-meshheading:2171427-Substrate Specificity, pubmed-meshheading:2171427-beta-Naphthoflavone
pubmed:year
1990
pubmed:articleTitle
Purification and characterization of cytochrome P450 isozymes from beta-naphthoflavone-induced adult hen liver.
pubmed:affiliation
Department of Pharmacology, Duke University Medical Center, Durham, North Carolina.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.