Human Liver Cytochrome P-450 Related to a Rat Acetone-Inducible, Nitrosamine-Metabolizing Cytochrome P-450: Identification and Isolation

Pharmacology ◽  
1989 ◽  
Vol 39 (3) ◽  
pp. 137-144 ◽  
Author(s):  
Richard C. Robinson ◽  
Robert G.L. Shorr ◽  
Angela Varrichio ◽  
Sang S. Park ◽  
Harry V. Gelboin ◽  
...  
1987 ◽  
Vol 102 (3) ◽  
pp. 493-501 ◽  
Author(s):  
Sumie KAWANO ◽  
Tetsuya KAMATAKI ◽  
Toshio YASUMORI ◽  
Yasushi YAMAZOE ◽  
Ryuichi KATO

1979 ◽  
Vol 88 (3) ◽  
pp. 826-832 ◽  
Author(s):  
Ph. Beaune ◽  
P. Dansette ◽  
J.P. Flinois ◽  
S. Columelli ◽  
D. Mansuy ◽  
...  

1990 ◽  
Vol 11 ◽  
pp. S38
Author(s):  
D. Larrey ◽  
M. Bourdi ◽  
J. Nataf ◽  
J. Bernuau ◽  
D. Pessayre ◽  
...  

1987 ◽  
Vol 36 (14) ◽  
pp. 2421-2424 ◽  
Author(s):  
Jean Genève ◽  
Dominique Larrey ◽  
Gilles Amouyal ◽  
Jacques Belghiti ◽  
Dominique Pessayre

1987 ◽  
Vol 36 (6) ◽  
pp. 951-955 ◽  
Author(s):  
Marina Tinel ◽  
Jacques Belghiti ◽  
Veronique Descatoire ◽  
Gilles Amouyal ◽  
Philippe Letteron ◽  
...  

1987 ◽  
Vol 102 (5) ◽  
pp. 1075-1082 ◽  
Author(s):  
Toshio YASUMORI ◽  
Sumie KAWANO ◽  
Kiyoshi NAGATA ◽  
Miki SHIMADA ◽  
Yasushi YAMAZOE ◽  
...  

1990 ◽  
Vol 267 (2) ◽  
pp. 365-371 ◽  
Author(s):  
J S Miles ◽  
A W McLaren ◽  
L M Forrester ◽  
M J Glancey ◽  
M A Lang ◽  
...  

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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