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Titolo:
Effect of cadmium acetate on the conformation of lysozyme: Functional implications
Autore:
Olmo, R; Blanco, MD; Socorro, JM; Martin, JA; Teijon, JM;
Indirizzi:
Univ Complutense Madrid, Fac Med, Dept Bioquim & Biol Mol, E-28040 Madrid,Spain Univ Complutense Madrid Madrid Spain E-28040 l Mol, E-28040 Madrid,Spain
Titolo Testata:
JOURNAL OF ENZYME INHIBITION
fascicolo: 1, volume: 16, anno: 2001,
pagine: 65 - 80
SICI:
8755-5093(2001)16:1<65:EOCAOT>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE SERUM-ALBUMIN; PREFERENTIAL INTERACTIONS; POLY(ETHYL METHACRYLATE); PROTEIN SOLUBILITY; BINDING; SYSTEM; WATER; SOLVATION; MIXTURES; MERCURY;
Keywords:
lysozyme; cadmium; preferential interactions; viscosity; secondary structure; enzyme inhibition; kinetics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Teijon, JM Univ Complutense Madrid, Fac Med, Dept Bioquim & Biol Mol, E-28040 Madrid,Spain Univ Complutense Madrid Madrid Spain E-28040 040 Madrid,Spain
Citazione:
R. Olmo et al., "Effect of cadmium acetate on the conformation of lysozyme: Functional implications", J ENZ INHIB, 16(1), 2001, pp. 65-80

Abstract

Structural variations of lysozyme as a consequence of its interaction withCdAc2, as well as the implications on the protein functionality have been studied. Variations in the conformation of the macromolecule are seen, however these changes are not reflected on the secondary structure. The interaction of the salt with the polypeptide chain is weak and thermodynamically unfavourable. Molecular aggregates (dimer forms) are observed at the highestsalt concentrations. This interaction causes an inhibitory effect on lysozyme, the activity loss being 50% at the highest salt concentration studied. The inhibition is of mixed type with an uncompetitive component. Thus cadmium does not bind to the active site of the enzyme which is in accordance with the not very large activity loss observed. The substrate inhibition of lysozyme is favoured in the presence of the salt, so interaction with the macromolecule is at low affinity sites.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 05:45:09