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

Karl J. Kramer, Larry L. Sanburg, Ferenc J. Kezdy and John H. Law
Proceedings of the National Academy of Sciences of the United States of America
Vol. 71, No. 2 (Feb., 1974), pp. 493-497
Stable URL: http://www.jstor.org/stable/62803
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
The Juvenile Hormone Binding Protein in the Hemolymph of Manduca sexta Johannson (Lepidoptera: Sphingidae)
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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.

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