1995
DOI: 10.1002/arch.940290408
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Identification, characterization, and developmental profile of a high molecular weight, juvenile hormone‐binding protein in the hemolymph of the migratory grasshopper, Melanoplus sanguinipes

Abstract: In the hemolymph of Melanoplus sanguinipes, a high molecular weight juvenile hormone binding protein (JHBP) was identified by photoaffinity labelling and found to have a M, of 480,000. The JHBF', purified using native gel electrophoresis followed by electroelution, has an equilibrium dissociation constant for JH Ill of 2.1 n M and preferentially binds JH Ill over JH I. Antibody raised against JHBP recognized only the 480,000 band. Under denaturing conditions the native JHBP gave a single band with a M, 78,000.… Show more

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Cited by 20 publications
(14 citation statements)
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“…This JHBP is a minor protein in the hemolymph (1-2% of total hemolymph protein), but the concentration of binding sites in the hemolymph is high (11-26 pM), due to its hexameric structure. A JHBP with similar characteristics was recently described for the grasshopper, Melanoplus sanguinipes (Ismail and Gillott, 1995). These two independent studies suggest that orthopterans have a distinct class of JHIII-specific binding protein.…”
Section: Juvenile Hormone Binding Proteinssupporting
confidence: 71%
“…This JHBP is a minor protein in the hemolymph (1-2% of total hemolymph protein), but the concentration of binding sites in the hemolymph is high (11-26 pM), due to its hexameric structure. A JHBP with similar characteristics was recently described for the grasshopper, Melanoplus sanguinipes (Ismail and Gillott, 1995). These two independent studies suggest that orthopterans have a distinct class of JHIII-specific binding protein.…”
Section: Juvenile Hormone Binding Proteinssupporting
confidence: 71%
“…Manual annotation showed that these PPO-like sequences consist of three conserved domains, Hemocyanin_N, Hemocyanin_C and the copper-containing Hemocyanin_M. But NCBI blast results suggested that they were more homologous to hexamerin storage protein, which are hemocyanin-derived proteins with functions in amino acid storage 55 56 , juvenile hormone (JH) binding 57 and in reproduction and metamorphosis 58 . Functional analysis needs to be performed to identify the actual roles of these proteins in P. xylostella .…”
Section: Resultsmentioning
confidence: 99%
“…In male M. sanguinipes, JH I11 is the sole identifiable product of the corpora allata (Couche et al, 1985). As in other insects, JH is transported through the hemolymph to its site of action bound to a hexameric, 480 kDa protein (Ismail and Gillott, 1995b). On reaching the long hyaline tubule, JH becomes associated with a 40 kDa, high affinity, cytosolic binding protein (Ismail and Gillott, 1994).…”
Section: Endocrine Control Of Mag Secretory Activitymentioning
confidence: 99%