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Titolo:
DIFFERENTIAL SCANNING CALORIMETRIC STUDIES ON THE THERMAL UNFOLDING OF PSEUDOMONAS-CEPACIA LIPASE IN THE ABSENCE AND PRESENCE OF ALCOHOLS
Autore:
TANAKA A;
Indirizzi:
MIE UNIV,FAC BIORESOURCES,LAB MOL BIOINFORMAT TSU MIE 5140008 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 2, volume: 123, anno: 1998,
pagine: 289 - 293
SICI:
0021-924X(1998)123:2<289:DSCSOT>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT DENATURATION; CRYSTAL-STRUCTURE; BACTERIAL LIPASE; PROTEINS; RIBONUCLEASE; ACTIVATION; RESOLUTION; CHAPERONE; ASPARTATE; LYSOZYME;
Keywords:
ALCOHOL; CALORIMETRY; DSC; PSEUDOMONAS CEPACIA LIPASE; THERMAL UNFOLDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
A. Tanaka, "DIFFERENTIAL SCANNING CALORIMETRIC STUDIES ON THE THERMAL UNFOLDING OF PSEUDOMONAS-CEPACIA LIPASE IN THE ABSENCE AND PRESENCE OF ALCOHOLS", Journal of Biochemistry, 123(2), 1998, pp. 289-293

Abstract

Thermal unfolding of Pseudomonas cepacia lipase (PCL) was studied by differential scanning calorimetry (DSC) at pH 7. The peak temperature t(p) of the DSC trace increased with increasing concentration of the protein. The DSC traces could be successfully analyzed on the basis of the following mechanism, assuming the dissociation of a calcium ion upon denaturation; N Ca(2+)reversible arrow D + Ca2+, where N and D represent native and denatured states of PCL, respectively. In the presence of 1-5% alcohols (methanol, ethanol, n-propanol, and n-butanol), t(p) decreased with increasing alcohol concentration and longer alkyl chain. In contrast to the case of t(p), the denaturation enthalpy Delta hdid not depend on the protein concentration or alcohol concentration used. The change in heat capacity on denaturation, Delta c(p)(d), evaluated directly from the DSC traces, was close to zero both in the absence or presence of alcohol, which could be due to the open conformation of the enzyme exposing a large hydrophobic surface to the solvent.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 22:24:33