Cimetidine and ranitidine: Their interaction with human and pig liver microsomes and withpurified cytochrome P-450

1984 ◽  
Vol 9 (3) ◽  
pp. 195-200 ◽  
Author(s):  
S. Rendić ◽  
H. H. Ruf ◽  
P. Weber ◽  
F. Kajfež
Keyword(s):  
Liver Microsomes ◽  
Pig Liver ◽  
Cytochrome P 450

scholarly journals Purification and characterization of a vitamin D3 25-hydroxylase from pig liver microsomes

1992 ◽  
Vol 287 (3) ◽  
pp. 725-731 ◽  
Author(s):  
E Axén ◽  
T Bergman ◽  
K Wikvall
Keyword(s):  
Liver Enzyme ◽  
Rat Liver ◽  
Vitamin D3 ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Pig Liver ◽  
Specific Content ◽  
Apparent Homogeneity ◽  
Structural And Functional Properties ◽  
Cytochrome P 450

A cytochrome P-450 which catalyses 25-hydroxylation of vitamin D3 has been purified to apparent homogeneity from pig liver microsomes. The specific content of cytochrome P-450 was 12 nmol.mg of protein-1, and the preparation showed a single band with an apparent M(r) of 50,500 upon SDS/PAGE. A monoclonal antibody raised against the vitamin D3 25-hydroxylase reacted strongly with the purified 25-hydroxylating cytochrome P-450 from pig kidney microsomes [Bergman & Postlind (1990) Biochem. J. 270, 345-350]. The liver enzyme showed structural and functional properties very similar to those of the kidney enzyme. The two enzymes differed with respect to only one of the first 16 N-terminal amino acids. The vitamin D3 25-hydroxylase in pig liver microsomes exhibited a turnover and an apparent Km for 25-hydroxylation of vitamin D3 which were of the same order of magnitude as those of a well-characterized male-specific 25-hydroxylating cytochrome P-450 in rat liver microsomes. The two enzymes differed structurally. The pig liver enzyme was, in contrast to the rat liver enzyme, not sex-specific, and did not catalyse 16 alpha-hydroxylation of testosterone. These properties of the 25-hydroxylase in rat liver microsomes have led to questions on the role of microsomal 25-hydroxylation of vitamin D3. It is concluded that studies on microsomal 25-hydroxylation with the rat may be misleading. The results of the present study show that the pig appears to be a representative species for evaluation of vitamin D3 hydroxylases in other mammals, including man.

Sulphoxidation of albendazole by the FAD-containing and cytochrome P-450 dependent mono-oxygenases from pig liver microsomes

Xenobiotica ◽  
1987 ◽  
Vol 17 (10) ◽  
pp. 1159-1168 ◽  
Author(s):  
H. Souhaili El Amri ◽  
X. Fargetton ◽  
P. Delatour ◽  
A. M. Batt
Keyword(s):  
Liver Microsomes ◽  
Pig Liver ◽  
Cytochrome P 450

scholarly journals Characterization of pig kidney microsomal cytochrome P-450 catalysing 25-hydroxylation of vitamin D3 and C27 steroids

1990 ◽  
Vol 270 (2) ◽  
pp. 345-350 ◽  
Author(s):  
T Bergman ◽  
H Postlind
Keyword(s):  
Vitamin D3 ◽  
Lauric Acid ◽  
Liver Microsomes ◽  
Hydroxylase Activity ◽  
Pig Liver ◽  
Pig Kidney ◽  
Sds Page ◽  
Kidney Microsomes ◽  
Alpha 7 ◽  
Cytochrome P 450

The cytochrome P-450 enzyme which catalyses 25-hydroxylation of vitamin D3 (cytochrome P-450(25] from pig kidney microsomes [Postlind & Wikvall (1988) Biochem. J. 253, 549-552] has been further purified. The specific content of cytochrome P-450 was 15.0 nmol.mg of protein-1, and the protein showed a single spot with an apparent isoelectric point of 7.4 and an Mr of 50,500 upon two-dimensional isoelectric-focusing/SDS/PAGE. The 25-hydroxylase activity towards vitamin D3 was 124 pmol.min-1.nmol of cytochrome P-450-1 and towards 1 alpha-hydroxyvitamin D3 it was 1375 pmol.min-1.nmol-1. The preparation also catalysed the 25-hydroxylation of 5 beta-cholestane-3 alpha,7 alpha-diol at a rate of 1000 pmol.min-1.nmol of cytochrome P-450-1 and omega-1 hydroxylation of lauric acid at a rate of 200 pmol.min-1.nmol of cytochrome P-450-1. A monoclonal antibody raised against the 25-hydroxylating cytochrome P-450, designated mAb 25E5, was prepared. After coupling to Sepharose, the antibody was able to bind to cytochrome P-450(25) from kidney as well as from pig liver microsomes, and to immunoprecipitate the activity for 25-hydroxylation of vitamin D3 and 5 beta-cholestane-3 alpha,7 alpha-diol when assayed in a reconstituted system. The hydroxylase activity towards lauric acid was not inhibited by the antibody. By SDS/PAGE and immunoblotting with mAb 25E5, cytochrome P-450(25) was detected in both pig kidney and pig liver microsomes. These results indicate a similar or the same species of cytochrome P-450 in pig kidney and liver microsomes catalysing 25-hydroxylation of vitamin D3 and C27 steroids. The N-terminal amino acid sequence of the purified cytochrome P-450(25) from pig kidney microsomes differed from those of hitherto isolated mammalian cytochromes P-450.

scholarly journals Specificity in the activation and inhibition by flavonoids of benzo[a]pyrene hydroxylation by cytochrome P-450 isozymes from rabbit liver microsomes.

1981 ◽  
Vol 256 (21) ◽  
pp. 10897-10901 ◽  
Author(s):  
M.T. Huang ◽  
E.F. Johnson ◽  
U. Muller-Eberhard ◽  
D.R. Koop ◽  
M.J. Coon ◽  
...  
Keyword(s):  
Liver Microsomes ◽  
Rabbit Liver ◽  
Cytochrome P 450

scholarly journals Ethanol Oxidation by a Component of Liver Microsomes Rich in Cytochrome P-450

1973 ◽  
Vol 248 (4) ◽  
pp. 1183-1187
Author(s):  
Esteban Mezey ◽  
James J. Potter ◽  
W. Douglas Reed
Keyword(s):  
Ethanol Oxidation ◽  
Liver Microsomes ◽  
Cytochrome P 450
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