Abstract
The lipid droplet fractions from rat adrenal and bovine adrenocortical tissue were isolated by density ultracentrifugation. The droplet fractions were delipidated and the protein components investigated by SDS-polyacrylamide slab gel electrophoresis. The adrenal lipid droplets from both species displayed a qualitatively similar protein profile, and both contained a major apolipoprotein subunit of M r 40000. Incubation of intact, non-delipidated lipid droplets with [γ- 32P]ATP in vitro resulted in the phosphorylation of the M r 40000 apolipoprotein subunit in the case of rat lipid droplets, but not in the case of bovine lipid droplets. However, following delipidation of the droplets with diethyl ether/ethanol, the M r 40000 apolipoprotein subunit was phosphorylated in both cases upon incubation of the delipidated protein fractions with [γ- 32P]ATP in vitro. Labelling with [γ- 32P]ATP and [ 3H]diisopropyl phosphorofluoridate indicated that the cholesterol ester hydrolase enzyme protein was not a major constituent of the adrenal lipid droplet protein fraction.
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