Premium
Long chain fatty acid methyl ester hydrolase activity in mammalian cells
Author(s) -
Spector Arthur A.,
Soboroff Janice M.
Publication year - 1972
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/bf02533061
Subject(s) - chemistry , enzyme , microsome , biochemistry , hydrolysis , hydrolase , fatty acid , albumin , clinical chemistry , enzyme assay , chromatography
Long chain fatty acid methyl esters were hydrolyzed by cell free homogenates and subcellular fractions prepared from Ehrlich ascites tumor cells. The highest enzyme specific activity was observed in the microsomal fraction. Maximum hydrolase activity occurred in the pH range of 6.5–7.0. The relative activities for the methyl ester substrates that we tested were: methyl palmitate > methyl laurate > methyl oleate > methyl stea‐rate. Butyl palmitate also was hydrolyzed by this enzyme. Enzymatic activity increased when the methyl ester‐albumin complex concentration or the methyl ester‐albumin molar ratio was raised. In addition to Ehrlich cells, methyl ester hydrolase activity was observed in homogenates of rat heart and liver. The highest enzyme specific activities also occurred in the microsomal fractions prepared from these tissues.