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The acylation of 1‐palmitylglycerol 3‐phosphate with Cis and Trans C‐16 to C‐22 monoenoic fatty acids in rat liver microsomes
Author(s) -
Marchand C. M.,
BeareRogers J. L.
Publication year - 1978
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/bf02533723
Subject(s) - clinical chemistry , microsome , enzyme , bovine serum albumin , acyltransferase , acylation , acyl coa , chemistry , biochemistry , acyltransferases , cis–trans isomerism , albumin , stereochemistry , chromatography , biosynthesis , catalysis
The configurational specificity of acyl‐CoA: 1‐palmitylglycerol 3‐phosphate acyltransferase from rat liver microsomes was investigated with cis and trans C‐16, C‐18, C‐20, and C‐22 monoenoic and saturated fatty acyl‐CoA. Oleyl‐CoA was transferred three times more readily than elaidyl‐CoA. Elaidyl‐CoA was more inhibitory than oleyl‐CoA, especially at low protein concentrations, but did not show this effect after the addition of 1 mg/ml bovine serum albumin (BSA). BSA permitted linearity of the acyltransferase over a wide range of protein concentrations and did not seem to affect the configurational specificity of the acyltransferase. The specificity of the enzyme preparation was in the following decreasing order: 18∶1 cis >16∶1 cis ≅16∶0>18∶0≅16∶1 trans >18∶1 trans >20∶1 cis >20∶1 trans . The enzyme preparation did not react with cis or trans 22∶1 acyl‐CoA.