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. 1974 Feb;71(2):493–497. doi: 10.1073/pnas.71.2.493

The Juvenile Hormone Binding Protein in the Hemolymph of Manduca sexta Johannson (Lepidoptera: Sphingidae)

Karl J Kramer 1, Larry L Sanburg 1, Ferenc J Kézdy 1, John H Law 1
PMCID: PMC388033  PMID: 16592141

Abstract

C18:juvenile hormone is quite soluble in water, yielding a monomeric solution greater than 10-5 M. In vivo injection or addition of aqueous juvenile hormone to the hemolymph in vitro shows the complexation of juvenile hormone to a protein, as demonstrated by gel permeation chromatography and disc-gel electrophoresis. The protein has an apparent molecular weight of 3.4 × 104 and is present in the hemolymph at a concentration in the micromolar range. The binding of the hormone to the protein can be described as a simple thermodynamic equilibrium with a dissociation constant of 3 × 10-7 M, and the protein has a much higher affinity for the hormone than for the hydrolysis products.

Keywords: tobacco hornworm, dissociation constant, specificity, esterases, diisopropylphosphofluoridate

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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