Abstract
THE discovery of a binding protein, specific for juvenile hormone (JH)1 in the haemolymph of the tobacco hornworm, Manduca sexta, suggested that this protein carries JH molecules from the secretory organs (corpora allata) to the target sites. We report here that the binding protein provides the hormone total protection from degradative enzymes present in the haemolymph throughout early larval life2,3. Just before the start of pupal differentiation, however, a new esterase appears in the haemolymph which is able to hydrolyse the protein-bound hormone. We have also found that the binding protein at concentrations of 10−8 M strongly enhances the development-inhibiting action of JH on wing disk tissue in vitro. These properties, taken together, demonstrate a carrier role for the binding protein, and give new insights into the control of hormone levels in the haemolymph.
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References
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SANBURG, L., KRAMER, K., KEZDY, F. et al. Role of juvenile hormone esterases and carrier proteins in insect development. Nature 253, 266–267 (1975). https://doi.org/10.1038/253266a0
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DOI: https://doi.org/10.1038/253266a0
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