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

Karl J. Kramer | Zendy; Larry L. Sanburg | Zendy; Ferenc J. Kézdy | Zendy; John H. Law | Zendy

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

Author(s) -

Karl J. Kramer,

Larry L. Sanburg,

Ferenc J. Kézdy,

John H. Law

Publication year - 1974

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.71.2.493

Subject(s) - manduca sexta , hemolymph , sphingidae , juvenile hormone , manduca , biochemistry , biology , dissociation constant , chromatography , chemistry , hormone , insect , botany , receptor

C(18):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 x 10(4) 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 x 10(-7) M, and the protein has a much higher affinity for the hormone than for the hydrolysis products.

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