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Titolo:
FLUORESCENCE SPECTROMETRY IN STUDIES OF CARBOHYDRATE-PROTEIN INTERACTIONS
Autore:
LEE YC;
Indirizzi:
JOHNS HOPKINS UNIV,DEPT BIOL BALTIMORE MD 21218
Titolo Testata:
Journal of Biochemistry
fascicolo: 5, volume: 121, anno: 1997,
pagine: 818 - 825
SICI:
0021-924X(1997)121:5<818:FSISOC>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
BEAN PSOPHOCARPUS-TETRAGONOLOBUS; LECTIN AFFINITY ELECTROPHORESIS; CAPILLARY ELECTROPHORESIS; TRIANTENNARY GLYCOPEPTIDE; CERAMIDE-GLYCANASE; ENERGY-TRANSFER; ERYTHRINA-CRISTAGALLI; BINDING CONSTANTS; ALPHA-AMYLASE; STOPPED-FLOW;
Keywords:
ENERGY TRANSFER; CONFORMATION; GLYCOPEPTIDES; SUBSTRATES;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
65
Recensione:
Indirizzi per estratti:
Citazione:
Y.C. Lee, "FLUORESCENCE SPECTROMETRY IN STUDIES OF CARBOHYDRATE-PROTEIN INTERACTIONS", Journal of Biochemistry, 121(5), 1997, pp. 818-825

Abstract

Fluorometric spectroscopy is a powerful tool for investigating the interaction between a carbohydrate ligand and binding proteins. The measurement is done in situ and thus circumventing the need for separationof bound ligand from the free ligand. The source of the fluorophore can be intrinsic, i.e., the tryptophan in the protein, or extrinsic (contained in the ligand). Techniques for assessing the affinity used aremeasurement on fluorescence intensity change, lifetime, polarization anisotropy, and energy transfer, The last technique can also be used to study conformational structures of glycopeptides. It is also useful in designing substrates for endo-type enzymes which allow continuous monitoring of the reaction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 13:11:06