A nuclear juvenile hormone-binding protein from larvae of Manduca sexta: a putative receptor for the metamorphic action of juvenile hormone.
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A nuclear juvenile hormone-binding protein from larvae of Manduca sexta: a putative receptor for the metamorphic action of juvenile hormone.
A 29-kDa nuclear juvenile hormone (JH)-binding protein from the epidermis of Manduca sexta larvae was purified by using the photoaffinity analog for JH II ([3H]epoxyhomofarnesyldiazoacetate) and partially sequenced. A 1.1-kb cDNA was isolated by using degenerate oligonucleotide primers for PCR based on these sequences. The cDNA encoded a 262-amino acid protein that showed no similarity with oth...
متن کاملThe Juvenile Hormone Binding Protein in the Hemolymph of Manduca sexta Johannson (Lepidoptera: Sphingidae).
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...
متن کاملIsolation, Structure, and Absolute Configuration of a New Natural Insect Juvenile Hormone from Manduca sexta.
Two juvenile hormones are isolated from organ cultures of corpora allata of the tobacco hornworm moth, Manduca sexta Johannson, and are purified by high-resolution liquid chromatography. These are identified as methyl (2E, 6E)-(10R)-10,11-epoxy-3,7,11-trimethyl-2,6-dodecadienoate, a new natural hormone, and methyl (2E,6E) - (10R,11S) - 10,11 - epoxy - 3,7,11 - trimethyl-2,6-tridecadienoate. [(1...
متن کاملLigand blot analysis of juvenile hormone esterase binding proteins in Manduca sexta L.
Biotinylated recombinant juvenile hormone esterase (JHE) was used for ligand blotting of proteins from fat body tissue and pericardial athrocytes of Manduca sexta. Proteins were separated by SDS-polyacrylamide gel electrophoresis or by two-dimensional electrophoresis. Eight putative JHE binding proteins were detected in fat body tissue and in pericardial athrocytes of both M. sexta and Heliothi...
متن کاملCharacterization of affinity-purified juvenile hormone esterase from the plasma of the tobacco hornworm, Manduca sexta.
Juvenile hormone (JH) esterase found primarily in the hemolymph and tissues of insects is a low abundance protein involved in the ester hydrolysis of insect juvenile hormones, JHs. The enzyme was purified from the larval plasma of wild-type Manduca sexta using an affinity column prepared by binding the ligand, 3-[(4'-mercapto)butylthio]-1,1,1-trifluoropropan-2-one (MBTFP), to epoxy-activated Se...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1994
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.91.13.6191