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Titolo:
Biochemical characterization of Wnt-Frizzled interactions using a soluble,biologically active vertebrate Wnt protein
Autore:
Hsieh, JC; Rattner, A; Smallwood, PM; Nathans, J;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 Genet, Baltimore, MD 21205 USA Johns5Hopkins Univ, Sch Med, Dept Neurosci & Ophthalmol, Baltimore, MD 2120 Johns Hopkins Univ Baltimore MD USA 21205 Ophthalmol, Baltimore, MD 2120 JohnsAHopkins Univ, Sch Med, Howard Hughes Med Inst, Baltimore, MD 21205 US Johns Hopkins Univ Baltimore MD USA 21205 ed Inst, Baltimore, MD 21205 US
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 7, volume: 96, anno: 1999,
pagine: 3546 - 3551
SICI:
0027-8424(19990330)96:7<3546:BCOWIU>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPEMANN ORGANIZER; BETA-CATENIN; WINGLESS PROTEIN; TISSUE POLARITY; XENOPUS EMBRYOS; CELL-SURFACE; DROSOPHILA; FAMILY; ENCODES; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Nathans, J Johns,Hopkins Univ, Sch Med, Dept Mol Biol & Genet, 805 PCTB,725 N Wolfe St Johns Hopkins Univ 805 PCTB,725 N Wolfe St Baltimore MD USA 21205
Citazione:
J.C. Hsieh et al., "Biochemical characterization of Wnt-Frizzled interactions using a soluble,biologically active vertebrate Wnt protein", P NAS US, 96(7), 1999, pp. 3546-3551

Abstract

Biochemical studies of Wnt signaling have been hampered by difficulties inobtaining large quantities of soluble, biologically active Wnt proteins. In this paper, we report the production in Drosophila S2 cells of biologically active Xenopus Wnt8 (XWnt8). Epitope- or alkaline phosphatase-tagged XWnt8 proteins are secreted by concentrated S2 cells in a form that is suitable for quantitative biochemical experiments with yields of 5 and 0.5 mg per liter, respectively. Conditions also are described for the production in 293 cells of an IgG fusion of the cysteine-rich domain (CRD) of mouse Frizzled 8 with a yield of 20 mg/liter. We demonstrate the use of these proteins for studying the interactions between soluble XWnt8 and various Frizzled proteins, membrane anchored or secreted CRDs, and a set of insertion mutants in the CRD of Drosophila Frizzled 2. In a solid phase binding assay, the affinity of the XWnt8-alkaline phosphatase Fusion for the purified mouse Frizzled 8-CRD-IgG fusion is approximate to 9 nM.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 20:49:40