Premium
Palmitoyl‐CoA synthetase on the external surface of isolated rat hepatocytes
Author(s) -
de Groote Katrien,
Velghe Griet,
Stals Hedwig K.,
Baes Myriam I.,
Declercq Peter E.
Publication year - 1996
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.691
Subject(s) - chemistry , biophysics , hepatocyte , microbiology and biotechnology , biochemistry , biology , in vitro
After incubating isolated rat hepatocytes with [1‐ 14 C]palmitic acid, CoA and ATP (+MgCl 2 ), a significant amount of [1‐ 14 C]palmitoyl‐CoA was found in the incubation medium. There was no correlation between its rate of synthesis and the degree of intactness of the cells. The results indicate that there is a long‐chain fatty acyl‐CoA synthetase active on the external surface of the hepatocyte plasma membrane. The activity of this enzyme was negligible in primary cultures of rat hepatocytes, suggesting that the exofacial long‐chain acyl‐CoA synthetase is an artifact of the collagenase perfusion technique used to prepare the hepatocytes.