Abstract
An isozyme of cytochrome P450 was purified from liver microsomes of guinea pigs by HPLC with anion-exchange and hydroxylaptite columns. The isozyme showed a single band of 52 kdalton on sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Oxidation activities of the final preparation towards p-nitroanisole, aniline and d-benzphetamine were 1.3 to 15.4-fold comparing with those of microsomal fraction. This isozyme was also concerned with oxidation of Δ9-tetrahydrocannabinol (THC) to 8α-hydroxy- (8α-OH-), 2′-OH- and 3′-OH-Δ9-THCs. The N-terminal region of the isozyme was considerably hydrophobic, and 13 of the first 20 amino acid residues was leucine. Since this first 20 amino acid sequence is 80% homologous with that of cytochrome P450 LM2 purified from rabbit liver microsomes, this isozyme can be categorized to a subfamily of P450 IIB.
| Original language | English |
|---|---|
| Pages (from-to) | 607-613 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 172 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Oct 30 1990 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Purification of a cytochrome P450 isozyme belonging to a subfamily of P450 IIB from liver microsomes of guinea pigs. / Narimatus, Shizuo; Akutsu, Yuko; Matsunaga, Tamihide; Watanabe, Kazuhito; Yamamoto, Ikuo; Yoshimura, Hidetoshi.
In: Biochemical and Biophysical Research Communications, Vol. 172, No. 2, 30.10.1990, p. 607-613.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification of a cytochrome P450 isozyme belonging to a subfamily of P450 IIB from liver microsomes of guinea pigs
AU - Narimatus, Shizuo
AU - Akutsu, Yuko
AU - Matsunaga, Tamihide
AU - Watanabe, Kazuhito
AU - Yamamoto, Ikuo
AU - Yoshimura, Hidetoshi
PY - 1990/10/30
Y1 - 1990/10/30
N2 - An isozyme of cytochrome P450 was purified from liver microsomes of guinea pigs by HPLC with anion-exchange and hydroxylaptite columns. The isozyme showed a single band of 52 kdalton on sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Oxidation activities of the final preparation towards p-nitroanisole, aniline and d-benzphetamine were 1.3 to 15.4-fold comparing with those of microsomal fraction. This isozyme was also concerned with oxidation of Δ9-tetrahydrocannabinol (THC) to 8α-hydroxy- (8α-OH-), 2′-OH- and 3′-OH-Δ9-THCs. The N-terminal region of the isozyme was considerably hydrophobic, and 13 of the first 20 amino acid residues was leucine. Since this first 20 amino acid sequence is 80% homologous with that of cytochrome P450 LM2 purified from rabbit liver microsomes, this isozyme can be categorized to a subfamily of P450 IIB.
AB - An isozyme of cytochrome P450 was purified from liver microsomes of guinea pigs by HPLC with anion-exchange and hydroxylaptite columns. The isozyme showed a single band of 52 kdalton on sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Oxidation activities of the final preparation towards p-nitroanisole, aniline and d-benzphetamine were 1.3 to 15.4-fold comparing with those of microsomal fraction. This isozyme was also concerned with oxidation of Δ9-tetrahydrocannabinol (THC) to 8α-hydroxy- (8α-OH-), 2′-OH- and 3′-OH-Δ9-THCs. The N-terminal region of the isozyme was considerably hydrophobic, and 13 of the first 20 amino acid residues was leucine. Since this first 20 amino acid sequence is 80% homologous with that of cytochrome P450 LM2 purified from rabbit liver microsomes, this isozyme can be categorized to a subfamily of P450 IIB.
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U2 - 10.1016/0006-291X(90)90717-2
DO - 10.1016/0006-291X(90)90717-2
M3 - Article
C2 - 2173574
AN - SCOPUS:0025184854
VL - 172
SP - 607
EP - 613
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -