Measurement of acetyl-CoA carboxylase activity in isolated hepatocytes
C Bijleveld, MJH Geelen - Biochimica et Biophysica Acta (BBA)-Lipids and …, 1987 - Elsevier
An assay is described for acetyl-CoA carboxylase activity in isolated hepatocytes. The assay
is based on two principles:(a) The hepatocytes are made permeable by digitonin. 64 μg of
digitonin per mg of cellular protein were most effective in exposing enzyme activity without a
significant effect on mitochondrial permeability.(b) Enzyme activity is measured by coupling
the carboxylase reaction to the fatty acid synthase reaction. The advantages offered by this
procedure over existing assays are:(i) rapidity,(ii) no need to prepare cell extracts,(iii) …
is based on two principles:(a) The hepatocytes are made permeable by digitonin. 64 μg of
digitonin per mg of cellular protein were most effective in exposing enzyme activity without a
significant effect on mitochondrial permeability.(b) Enzyme activity is measured by coupling
the carboxylase reaction to the fatty acid synthase reaction. The advantages offered by this
procedure over existing assays are:(i) rapidity,(ii) no need to prepare cell extracts,(iii) …
