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Incubation of rat adipocytes with the same range of noradrenaline concentrations that stimulate lipolysis caused a rapid and stable decrease in the activity of fatty acyl-CoA synthetase. Corticotropin, glucagon and dibutyryl cyclic AMP also decreased the activity of the enzyme. The effect of noradrenaline was apparent over a wide range of concentrations for the three substrates of the enzyme. A novel fluorescence assay of fatty acyl-CoA synthetase using (1,N6-etheno)-CoA is described. The effect of noradrenaline was not abolished by inclusion of albumin in homogenization buffers, persisted through subcellular fractionation and isolation of microsomes (microsomal fractions) and even survived treatment of microsomes with Triton X-100. The effect of noradrenaline was rapidly reversed within cells by the subsequent addition of insulin or propranolol. The inclusion of fluoride in homogenization buffers did not alter the observed effect of noradrenaline. Additions of cyclic AMP-dependent protein kinase to adipocyte microsomes caused considerable phosphorylation of microsomal protein by [gamma-32P]ATP, but did not affect the activity of fatty acyl-CoA synthetase.
M Hall, and
E D Saggerson
January 1975,
Methods in enzymology,
M Hall, and
E D Saggerson
August 1978,
FEBS letters,
M Hall, and
E D Saggerson
January 2016,
Methods in molecular biology (Clifton, N.J.),
M Hall, and
E D Saggerson
January 1981,
Methods in enzymology,
M Hall, and
E D Saggerson
June 1992,
Journal of cardiovascular pharmacology,
M Hall, and
E D Saggerson
June 1996,
Molecular and cellular biochemistry,
M Hall, and
E D Saggerson
February 1983,
Biochimica et biophysica acta,
M Hall, and
E D Saggerson
July 2009,
The Journal of biological chemistry,
M Hall, and
E D Saggerson
June 1963,
Biochimica et biophysica acta,
M Hall, and
E D Saggerson
May 1990,
The Journal of biological chemistry,
