Premium
Hydroxylation of fatty acids and alcohols by hepatic microsomal cytochrome P‐450 system from the Mongolian gerbil
Author(s) -
Miura Yoshiro,
Hisaki Harumi,
Siems Werner,
Oda Senichi
Publication year - 1987
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536437
Subject(s) - microsome , hydroxylation , cytochrome , gerbil , chemistry , cytochrome p450 , biochemistry , lauric acid , microsoma , fatty acid , enzyme , medicine , ischemia
The liver microsomes of the Mongolian gerbil Meriones unguiculatus catalyzed the hydroxylation of various saturated fatty acids (C 8 −C 18 ), alcohols (C 12 and C 16 ) and hydrocarbon (C 12 ) to the corresponding ω‐ and (ω‐1)‐hydroxy derivatives. Lauric acid was hydroxylated most effectively among saturated fatty acids and the order of activity as hydroxylation substrates was C 12 >C 14 >C 13 >C 16 >C 10 >C 18 >C 8 . The specific activity of laurate hydroxylation (5.99 nmol/mg microsomal protein/min) in gerbil liver microsomes was higher than that observed in other species. 1‐Dodecanol was also hydroxylated very effectively (4.58 nmol/mg microsomal protein/min) by gerbil liver microsomes, but in general the hydroxylation rates for fatty alcohols were much lower than those for the corresponding acids. It was found from both inhibitor and cofactor studies that the enzyme catalyzing the hydroxylation of fatty acids and alcohols in the liver microsomes of the Mongolian gerbil was a typical cytochrome P‐450‐linked monooxygenase, and at least two different cytochrome P‐450 species were involved in the hydroxylation.