Abstract
Binding of juvenile hormone (JH) to haemolymph proteins in larvae of the Indian meal moth, Plodia interpunctella, was measured by using radiolabeled Hylaphora JH. The proteins were separated by gel permeation chromatography and disc gel electrophoresis. A protein with an estimated molecular weight of 2.5 × 10 4 selectively bound JH in vitro. Lipoproteins also bound the hormone but only when excess JH was present. We conclude that the lower mol. wt. JH binding protein serves as the actual carrier for JH in the larvae of this insect species.
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