Differential stability of baculovirus late transcription complexes during initiation and elongation

Oleosins are amphipathic proteins associated with oil bodies in seeds. We purified the major 16,500 peanut oleosin by preparative SDS-PAGE. Autoradiography after SDS-PAGE separation of the iodinated oleosin revealed covalently bound oligomers with Mr of 21,000, 33,000, 44,000 and 51,000. The strong capacity of these oligomers to form aggregates and to be incorporated into large-sized detergent micelles was demonstrated by gel permeation and isoelectric focusing. A 50% ethanol concentration was necessary to elute the 16,500 oleosin from octyl groups in hydrophobic interaction chromatography showing its natural tendency to interact with lipid acyl chains. This oligomerization behavior in aqueous solution is an indirect reflection of the interactions that occur in the oil body.