ω-1 and ω-2 hydroxylation of prostaglandins by rabbit hepatic microsomal cytochrome P-450 isozyme 6
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چکیده
منابع مشابه
Hydroxylation of prostaglandins by inducible isozymes of rabbit liver microsomal cytochrome P-450. Participation of cytochrome b5.
The hydroxylation of prostaglandin (PG) E1, PGE2, and PGA1 was investigated in a reconstituted rabbit liver microsomal enzyme system containing phenobarbital-inducible isozyme 2 or 5,6-benzoflavone-inducible isoenzyme 4 of P-450, NADPH-cytochrome P-450 reductase, phosphatidylcholine, and NADPH. Significant metabolism of prostaglandins by isozyme 2 occurred only in the presence of cytochrome b5....
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Cytochrome P-450 isozyme 2 from rabbit liver microsomes fluoresces upon excitation at 295 nm due to the single tryptophyl residue (Trp121) in the protein. The fluorescence spectrum, which is not altered by the presence of phospholipid or substrates, has a maximum at 335 nm, which suggests that the environment of the residue is hydrophobic. The fluorescence intensity decreases linearly with incr...
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Rabbit liver (male) microsomal metabolism of 10 MM|4,5,9,10-3H)-1nitropyrene (1NP) was investigated. The total metabolism was not ap preciably different with rates of 4.44 ±0.45, 3.98 ±0.19, 3.90 ±0.16, and 3.75 ±0.27 nmol/min/mg protein, respectively, for microsomes from phénobarbital,Aroclor-1254, ethanol-treated, and untreated rabbits. However, a more noticeable difference was found in ...
متن کاملOxidative metabolism of 1-nitropyrene by rabbit liver microsomes and purified microsomal cytochrome P-450 isozymes.
Rabbit liver (male) microsomal metabolism of 10 microM [4,5,9,10-3H]-1-nitropyrene (1NP) was investigated. The total metabolism was not appreciably different with rates of 4.44 +/- 0.45, 3.98 +/- 0.19, 3.90 +/- 0.16, and 3.75 +/- 0.27 nmol/min/mg protein, respectively, for microsomes from phenobarbital, Aroclor-1254, ethanol-treated, and untreated rabbits. However, a more noticeable difference ...
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Liver microsomes from rabbits treated chronically with ethanol were solubilized and fractionated to yield a new isozyme of cytochrome P-450 in a homogeneous state. This cytochrome, designated as isozyme 3a on the basis of its relative electrophoretic mobility, is distinct from the known terminal amino acid sequences. In addition, peptide mapping by high performance liquid chromatography followi...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 1985
ISSN: 0003-9861
DOI: 10.1016/0003-9861(85)90781-7