Abstract
Recently the interaction of juvenile hormone (JH) with hemolymph proteins has been the subject of intense investigation. There is an accumulating body of evidence indicating that specific carrier proteins interact with the hormone in the hemolymph to transport it from the site of synthesis, the corpora allata, to target cells. This transportation is necessary not because of the limited solubility of JH, but because of the presence of ubiquitous nonspecific esterases that degrade uncomplexed hormone. A specific JH-esterase has also been identified that hydrolyzes complexed hormone and lowers the JH titer at the end of larval growth, allowing metamorphosis to proceed.
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Kramer, K.J., Dunn, P.E., Peterson, R.C., Law, J.H. (1976). Interaction of Juvenile Hormone with Binding Proteins in Insect Hemolymph. In: Gilbert, L.I. (eds) The Juvenile Hormones. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7947-8_23
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DOI: https://doi.org/10.1007/978-1-4684-7947-8_23
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