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Titolo:
PRODUCTION AND CHARACTERIZATION OF A BIVALENT SINGLE-CHAIN FV ALKALINE-PHOSPHATASE CONJUGATE SPECIFIC FOR THE HEMOCYANIN OF THE SCORPION ANDROCTONUS-AUSTRALIS
Autore:
MOUSLI M; GOYFFON M; BILLIALD P;
Indirizzi:
MUSEUM NATL HIST NAT,57 RUE CUVIER F-75231 PARIS 05 FRANCE MUSEUM NATL HIST NAT F-75231 PARIS 05 FRANCE FAC PHARM TOURS F-37200 TOURS FRANCE
Titolo Testata:
Biochimica et biophysica acta (G). General subjects
fascicolo: 2, volume: 1425, anno: 1998,
pagine: 348 - 360
SICI:
0304-4165(1998)1425:2<348:PACOAB>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT COLORIMETRIC ANTIBODIES; ESCHERICHIA-COLI; FUSION PROTEIN; SEGMENTAL FLEXIBILITY; BACTERIAL EXPRESSION; QUATERNARY STRUCTURE; IMMUNOGLOBULIN-G; CONSTRUCTION; ENZYME; SUBUNIT;
Keywords:
HEMOCYANIN; SCFV; RECOMBINANT ANTIBODY; ALKALINE PHOSPHATASE; ELECTRON MICROSCOPY; (SCORPION);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
60
Recensione:
Indirizzi per estratti:
Citazione:
M. Mousli et al., "PRODUCTION AND CHARACTERIZATION OF A BIVALENT SINGLE-CHAIN FV ALKALINE-PHOSPHATASE CONJUGATE SPECIFIC FOR THE HEMOCYANIN OF THE SCORPION ANDROCTONUS-AUSTRALIS", Biochimica et biophysica acta (G). General subjects, 1425(2), 1998, pp. 348-360

Abstract

A102 is a monoclonal antibody raised against the hemocyanin of the Tunisian scorpion Androctonus australis. It is directed against the subunit Aa6 and does not cross-react when tested against a variety of similar scorpion hemocyanins. Here, we report the construction of a plasmid encoding a recombinant enzyme-linked antigen-binding protein with the antigen-binding specificity of antibody A102. The DNA fragments encoding the variable domains of A102 were inserted into a prokaryotic expression vector so as to produce a single chain antibody variable fragment (scFv) fused to the bacterial alkaline phosphatase. The fusion protein preserved the IgG binding and alkaline phosphatase activities. Immunoelectron microscopic analysis showed that the recombinant protein bound antigen bivalently as is the case for natural antibodies. Crude preparations containing the conjugate were used in a rapid visual immunoassay for the specific detection of ii. australis hemocyanin, using a droplet of hemolymph removed from live animals by puncture. The simplicity of the test made it suitable for the direct identification of animals belonging to this species, It could be useful in areas where A.australis, the most dangerous African scorpion, is found with other species from which it is not easy to distinguish using morphological criteria. (C) 1998 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/10/20 alle ore 03:02:52