Abstract
IT is now evident that α-ecdysone, a polyhydroxylated steroid, is synthesised and secreted by the insect prothoracic (ecdysial) glands1–3, β-ecdysone (20-hydroxy-α-ecdysone) seems, however, to have the major role in eliciting moulting during the post-embryonic development of insects4. If α-ecdysone functions as a pro(pre)-hormone as has been suggested1,4, then it must undergo hydroxylation at C-20 of the side chain to form the moulting hormone, β-ecdysone. This conversion of α- to β-ecdysone is carried out by a hydroxylase which is located in tissues peripheral to the prothoracic glands1,5,6. Little is known about the subcellular distribution of this enzyme complex and there is virtually no information regarding the type of enzyme complex responsible for the oxygenation of steroids in insects in general. Using the vertebrate mixed function oxidase system as a model, we have investigated the subcellular distribution and enzymatic characteristics of the insect C-20 hydroxylase in last instar larvae of the tobacco hornworm, Manduca sexta.
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BOLLENBACHER, W., SMITH, S., WIELGUS, J. et al. Evidence for an α-ecdysone cytochrome P-450 mixed function oxidase in insect fat body mitochondria. Nature 268, 660–663 (1977). https://doi.org/10.1038/268660a0
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DOI: https://doi.org/10.1038/268660a0
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