Catalytic and immunological comparison of coumarin 7-hydroxylation in different species

• Published in: Comparative biochemistry and physiology. C, Comparative pharmacology Vol. 81; no. 2; pp. 293 - 296
• Main Authors: Kaipainen, Pekka, Koivusaari, Ulla, Lang, Matti
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier B.V 1985; New York, NY Pergamon Press
• Subjects: Animals; Antibodies; Antigen-Antibody Complex; Applied sciences; Aryl Hydrocarbon Hydroxylases; Astacoidea; catalytic activity; coumarins; Cricetinae; Cytochrome P-450 CYP2A6; Exact sciences and technology; fish; Guinea Pigs; hamsters; immune response; Immunodiffusion; Mice; Mice, Inbred Strains; Microsomes, Liver - enzymology; Mixed Function Oxygenases - metabolism; Other techniques and industries; Rabbits; Rats; Species Specificity; Swine; Trout
• ISSN: 0306-4492; 0742-8413
• DOI: 10.1016/0742-8413(85)90008-8

1. 1. Coumarin 7-hydroxylation activities were determined in the liver microsomes of eight different species: pig, mouse (three strains), rat, hamster, guinea-pig, rabbit, rainbow trout and crayfish. 2. 2. A high coumarin 7-hydroxylase activity was found in the microsomes of D2 mouse, rabbit, hamster and pig, an intermediate activity in case of B6 and AKR mice, rat and guinea-pig and a very low activity in rainbow trout and crayfish. 3. 3. In Ouchterlony immunodiffusion analysis our antibody against coumarin 7-hydroxylase specific cytochrome P-450 from D2 mice was able to form a weak precipitin line only with rat and hamster microsomes in addition to the three strains of mice (D2, B6, AKR) where the band was very sharp. 4. 4. Strongest inhibition by the antibody (50% or more) of microsomal coumarin 7-hydroxylase was found in the case of the three strains of mice and rabbit. In the case of the other species the inhibition was very weak or did not exist.