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Fatty acid desaturase systems of hen liver and their inhibition by cyclopropene fatty acids
Author(s) -
Johnson A. R.,
Fogerty A. C.,
Pearson Judith A.,
Shenstone F. S.,
Bersten Audrey M.
Publication year - 1969
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/bf02533184
Subject(s) - cyclopropene , fatty acid , substrate (aquarium) , stearic acid , biochemistry , oleic acid , enzyme , free fatty acid receptor , chemistry , stereochemistry , polyunsaturated fatty acid , biology , organic chemistry , ecology
Hen liver preparations which desaturate stearic acid at the 9,10 position to form oleic acid have been found to desaturate other saturated fatty acids of carbon chain length from 12 to 20 and 22. The 9,10‐monoenoic fatty acid of the same chain length as the substrate fatty acid is the major product formed. Minor amounts of the 10,11‐ and 11, 12‐monoenoic acids are also formed. Maximum desaturation occurred with the C 14 fatty acid substrate and with the fatty acids C 17 and C 18 , suggesting the presence of at least two desaturating systems. The cyclopropene fatty acids, sterculic and malvalic acids, inhibited the desaturation of all thefatty acids at the 9,10 position but desaturation at the 10,11 and 11, 12 positions was affected only slightly. The effect is not due to inhibition of the primary activating enzyme, the long chain acyl CoA synthetase. Sterculic acid is a more effective inhibitor than either malvalic acid or sterculyl alcohol, probably because these cyclopropene compounds do not block the desaturating site of the enzyme as completely as sterculic acid.