Abstract
Metabolism of 2,5,2',5'-tetrachlorobiphenyl (TCB) was studied using liver microsomes of hamsters and two hamster P450 isoforms, CYP1A2 and 2A8. CYP2A8 catalyzed selectively 4-hydroxylation of 2,5,2',5-TCB at a rate of 21.7 pmol/min/nmol P450. In contrast, CYP1A2 showed no activity for hydroxylation of 2,5,2',5'-TCB. Immunological study revealed that rabbit antiserum against CYP2A8 almost completely inhibited the microsomal 4-hydroxylation but that against CYP1A2 did not. It was also shown that the induction pattern of CYP2A8 protein by P450 inducer was similar to that of the 4-hydroxylase activity in hamster liver microsomes. These results suggest that CYP2A8 plays a major role in the 4-hydroxylation of 2,5,2',5'-TCB in hamster liver.
| Original language | English |
|---|---|
| Pages (from-to) | 685-688 |
| Number of pages | 4 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 225 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Aug 14 1996 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Hamster liver cytochrome P450 (CYP2A8) as a 4-hydroxylase for 2,5,2',5'-tetrachlorobiphenyl. / Koga, Nobuyuki; Kikuichi, Naoko; Kanamaru, Tomoyo; Ariyoshi, Noritaka; Oguri, Kazuta; Yoshimura, Hidetoshi.
In: Biochemical and Biophysical Research Communications, Vol. 225, No. 2, 14.08.1996, p. 685-688.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hamster liver cytochrome P450 (CYP2A8) as a 4-hydroxylase for 2,5,2',5'-tetrachlorobiphenyl
AU - Koga, Nobuyuki
AU - Kikuichi, Naoko
AU - Kanamaru, Tomoyo
AU - Ariyoshi, Noritaka
AU - Oguri, Kazuta
AU - Yoshimura, Hidetoshi
PY - 1996/8/14
Y1 - 1996/8/14
N2 - Metabolism of 2,5,2',5'-tetrachlorobiphenyl (TCB) was studied using liver microsomes of hamsters and two hamster P450 isoforms, CYP1A2 and 2A8. CYP2A8 catalyzed selectively 4-hydroxylation of 2,5,2',5-TCB at a rate of 21.7 pmol/min/nmol P450. In contrast, CYP1A2 showed no activity for hydroxylation of 2,5,2',5'-TCB. Immunological study revealed that rabbit antiserum against CYP2A8 almost completely inhibited the microsomal 4-hydroxylation but that against CYP1A2 did not. It was also shown that the induction pattern of CYP2A8 protein by P450 inducer was similar to that of the 4-hydroxylase activity in hamster liver microsomes. These results suggest that CYP2A8 plays a major role in the 4-hydroxylation of 2,5,2',5'-TCB in hamster liver.
AB - Metabolism of 2,5,2',5'-tetrachlorobiphenyl (TCB) was studied using liver microsomes of hamsters and two hamster P450 isoforms, CYP1A2 and 2A8. CYP2A8 catalyzed selectively 4-hydroxylation of 2,5,2',5-TCB at a rate of 21.7 pmol/min/nmol P450. In contrast, CYP1A2 showed no activity for hydroxylation of 2,5,2',5'-TCB. Immunological study revealed that rabbit antiserum against CYP2A8 almost completely inhibited the microsomal 4-hydroxylation but that against CYP1A2 did not. It was also shown that the induction pattern of CYP2A8 protein by P450 inducer was similar to that of the 4-hydroxylase activity in hamster liver microsomes. These results suggest that CYP2A8 plays a major role in the 4-hydroxylation of 2,5,2',5'-TCB in hamster liver.
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UR - http://www.scopus.com/inward/citedby.url?scp=0030583243&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1996.1230
DO - 10.1006/bbrc.1996.1230
M3 - Article
C2 - 8753819
AN - SCOPUS:0030583243
VL - 225
SP - 685
EP - 688
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -