Comparison of CYP2A6 catalytic activity on coumarin 7-hydroxylation in human and monkey liver microsomes

1997 ◽  
Vol 22 (4) ◽  
pp. 295-304 ◽  
Author(s):  
Yan Li ◽  
Ning-Yuan Li ◽  
Edward M. Sellers
Keyword(s):  
Catalytic Activity ◽  
Liver Microsomes ◽  
Monkey Liver ◽  
Coumarin 7

Inhibition of Coumarin 7-Hydroxylase Activity in Human Liver Microsomes

1997 ◽  
Vol 341 (1) ◽  
pp. 47-61 ◽  
Author(s):  
Alison J. Draper ◽  
Ajay Madan ◽  
Andrew Parkinson
Keyword(s):  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
Hydroxylase Activity ◽  
Coumarin 7

Inhibition of cytochrome P450 2A participating in coumarin 7-hydroxylation in pig liver microsomes

2011 ◽  
Vol 34 (5) ◽  
pp. 424-429
Author(s):  
Z.-Y. LIU ◽  
M.-H. DAI ◽  
Y.-F. TAO ◽  
D.-M. CHEN ◽  
Z.-H. YUAN
Keyword(s):  
Cytochrome P450 ◽  
Liver Microsomes ◽  
Pig Liver ◽  
Coumarin 7

scholarly journals The Influence of Quinolines on Coumarin 7-Hydroxylation in Bovine Liver Microsomes and Human CYP2A6

2002 ◽  
Vol 48 (2) ◽  
pp. 118-125 ◽  
Author(s):  
Yoshie Hirano ◽  
Mayumi Uehara ◽  
Ken-ichi Saeki ◽  
Taka-aki Kato ◽  
Kazuhiko Takahashi ◽  
...  
Keyword(s):  
Liver Microsomes ◽  
Bovine Liver ◽  
Coumarin 7

scholarly journals Identification of the human liver cytochrome P-450 responsible for coumarin 7-hydroxylase activity

1990 ◽  
Vol 267 (2) ◽  
pp. 365-371 ◽  
Author(s):  
J S Miles ◽  
A W McLaren ◽  
L M Forrester ◽  
M J Glancey ◽  
M A Lang ◽  
...  
Keyword(s):  
Human Liver ◽  
Liver Microsomes ◽  
Microsomal Protein ◽  
Hydroxylase Activity ◽  
Liver Cytochrome ◽  
Partial Length ◽  
Coumarin 7 ◽  
Human Livers ◽  
Cell Expression ◽  
Cytochrome P 450

1. We have constructed a full-length human liver cytochrome P450IIA cDNA from a partial-length clone by oligonucleotide-directed mutagenesis, and subcloned it into the monkey kidney (COS-7) cell expression vector, pSVL. 2. The cDNA encodes a 49 kDa protein with coumarin 7-hydroxylase (COH) activity which cross-reacts with antisera to the mouse cytochrome P-450 isoenzyme responsible for COH activity and comigrates with a human liver microsomal protein. 3. Western blot analysis of a panel of human livers indicates that the level of the 49 kDa protein, detected using antisera to either the mouse COH P-450 or rat P450IIA1 protein, correlates very highly with COH activity. 4. Antisera to the rat P450IIA1 protein can inhibit COH activity in human liver microsomes. Taken together, these data indicate that a member of the P450IIA subfamily is responsible for most, if not all, of the COH activity in human liver.

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