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Titolo:
SIDE-CHAIN SELECTIVE AND COVALENT LABELING OF PROTEINS BY ORGANOMETALLIC COMPLEXES OF HEAVY TRANSITION-METALS - POSSIBLE APPLICATION IN RADIO-CRYSTALLOGRAPHY OF PROTEINS
Autore:
SALMAIN M; GORFTI A; JAOUEN G;
Indirizzi:
ECOLE NATL SUPER CHIM PARIS,LAB CHIM ORGANOMET,CNRS,UMR 7576,11 RUE PIERRE & MARIE CURIE F-75231 PARIS 05 FRANCE ECOLE NATL SUPER CHIM PARIS,LAB CHIM ORGANOMET,CNRS,UMR 7576 F-75231 PARIS 05 FRANCE
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 258, anno: 1998,
pagine: 192 - 199
SICI:
0014-2956(1998)258:1<192:SSACLO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
EGG-WHITE LYSOZYME; N-SUCCINIMIDYL; SURFACE-TOPOLOGY; BINDING ABILITY; SERUM-ALBUMIN; REAGENT; ESTERS;
Keywords:
BOVINE SERUM ALBUMIN; HEN EGG WHITE LYSOZYME; TRANSITION ORGANOMETALLIC COMPLEX; LABELING; STRUCTURAL BIOLOGY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M. Salmain et al., "SIDE-CHAIN SELECTIVE AND COVALENT LABELING OF PROTEINS BY ORGANOMETALLIC COMPLEXES OF HEAVY TRANSITION-METALS - POSSIBLE APPLICATION IN RADIO-CRYSTALLOGRAPHY OF PROTEINS", European journal of biochemistry, 258(1), 1998, pp. 192-199

Abstract

Organo-rhenium and organo-tungsten N-succinimidyl and N-sulfosuccinimidyl esters react at amino groups of proteins to form stable amide bonds between the protein and the heavy transition metal complexes. We show here that factors such as pH of the reaction medium and nature of the reagent (coordinating metal, surrounding ligands, type of ester) had a marked influence on the final number of coupled organometallic groups per protein molecule, defined as the coupling ratio. By operating with stoichiometric quantities of reagent with respect to the number of amino groups, up to 30 organometallic groups were introduced into the model protein, bovine serum albumin (BSA). BSA conjugates were characterized by gel electrophoresis in non-denaturating conditions. Hen egg-white lysozyme organo-tungsten conjugates were prepared in the same manner and the peptides resulting from their tryptic hydrolysis were analyzed by reverse-phase HPLC. A tentative assignment of the preferential amino sites of conjugation is suggested from the latter results.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 13:07:09