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Titolo:
PURIFICATION AND REASSESSMENT OF LIGAND-BINDING BY THE RECOMBINANT, PUTATIVE JUVENILE-HORMONE RECEPTOR OF THE TOBACCO HORNWORM, MANDUCA-SEXTA
Autore:
CHARLES JP; WOJTASEK H; LENTZ AJ; THOMAS BA; BONNING BC; PALLI SR; PARKER AG; DORMAN G; HAMMOCK BD; PRESTWICH GD; RIDDIFORD LM;
Indirizzi:
UNIV WASHINGTON,DEPT ZOOL,BOX 351800 SEATTLE WA 98195 UNIV WASHINGTON,DEPT ZOOL SEATTLE WA 98195 SUNY STONY BROOK,DEPT CHEM STONY BROOK NY 11794 UNIV CALIF DAVIS,DEPT ENTOMOL DAVIS CA 95616 UNIV CALIF DAVIS,DEPT ENVIRONM TOXICOL DAVIS CA 95616
Titolo Testata:
Archives of insect biochemistry and physiology
fascicolo: 4, volume: 31, anno: 1996,
pagine: 371 - 393
SICI:
0739-4462(1996)31:4<371:PAROLB>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR POLYHEDROSIS-VIRUS; DEVELOPMENTAL EXPRESSION; AFFINITY PURIFICATION; LARVAL EPIDERMIS; GENE-EXPRESSION; PROTEIN; ESTERASE; HEMOLYMPH; ANALOGS; ASSAY;
Keywords:
JUVENILE HORMONE RECEPTOR; PHOTOAFFINITY LABELING; TN5 CELLS; SF21 CELLS; CELLULAR ESTERASES; JH ESTERASE; RECOMBINANT BACULOVIRUS PROTEIN; MANDUCA SEXTA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Charles et al., "PURIFICATION AND REASSESSMENT OF LIGAND-BINDING BY THE RECOMBINANT, PUTATIVE JUVENILE-HORMONE RECEPTOR OF THE TOBACCO HORNWORM, MANDUCA-SEXTA", Archives of insect biochemistry and physiology, 31(4), 1996, pp. 371-393

Abstract

The 29 kDa protein from the larval epidermis of the tobacco hornworm,Manduca sexta, that specifically bound photoaffinity analogs of JH I and JH II was produced by a recombinant baculovirus (rJP29). The higher of the two molecular weight forms made corresponded to a protein that could be formed by read-through of the TGA termination codon to the following TAA. The previously reported, apparent high affinity bindingof [methyl-H-3]-JH I by rJP29 as measured by the dextran-coated charcoal (DCC) assay [Palli et al., Proc Natl Acad Sci USA 91:6191-6195 (1994)] was found to be artifactual due to endogenous cellular esterases that co-purifed with rJP29 through both DEAE cellulose and MonoQ chromatography. These esterases converted the 10-20 nM labelled JH to JH I acid and [H-3]-methanol during the 1 h incubation at room temperature. Additionally, DEAE fractions containing rJP29 or from wild-type virus-infected cells were found to bind nonspecifically high amounts of 12,13-H-3]-JH I acid in the DCC assay. Neither rJP29 nor the cellular esterases had JH esterase activity when assayed on a series of thioethersurrogate substrates. When separated from these contaminating esterases either by hydroxylapatite or affinity chromatography, rJP29 showed little or no detectable binding of [12,13-H-3]-JH I. Yet purified rJP29 bound EBDA, the photoaffinity analog of JH I; and this binding was prevented by retinol, JH I, methyl farnesoate, methoprene, and xanthophyll, but not by farnesol and 20-hydroxyecdysone. Therefore, JP29 is not a high affinity JH receptor. (C) 1996 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 15:53:31