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Titolo:
STUDIES ON CA2-AMYLASE( BINDING OF THERMOSTABLE ALPHA)
Autore:
ZHAO Y; FEI XF; ZHENG YJ; DONG QC; WANG J; CHENG G;
Indirizzi:
JILIN UNIV,DEPT MOL BIOL CHANGCHUN 130023 PEOPLES R CHINA
Titolo Testata:
Gaodeng xuexiao huaxue xuebao
fascicolo: 8, volume: 19, anno: 1998,
pagine: 1267 - 1270
SICI:
0251-0790(1998)19:8<1267:SOCBOT>2.0.ZU;2-0
Fonte:
ISI
Lingua:
CHI
Keywords:
ALPHA-AMYLASE; CA2+; CONFORMATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
5
Recensione:
Indirizzi per estratti:
Citazione:
Y. Zhao et al., "STUDIES ON CA2-AMYLASE( BINDING OF THERMOSTABLE ALPHA)", Gaodeng xuexiao huaxue xuebao, 19(8), 1998, pp. 1267-1270

Abstract

It was determined that alpha-amylase contained ten Ca2+. Resulted from the study of stability and activity of Ca2+-free alpha-amylase afteradding Ca2+, the first eight Ca2+ related to catalyt ic function of the enzyme, the other two Ca2+ made the structure of enzyme stable. According to the CD and fluorescence spectra of alpha-amylase at room temperature, no significant change of the enzyme structure was observed. Furthermore, according to the CD spectra of alpha-amylase after addingCa2+ (heated at 90 degrees C for 15 min), some alpha-helix structuresof the enzyme still existed. Fluorescence spectra of alpha-amylase at90 degrees C for 15 min also showed that enzyme kept the conformationmaximum stability when the Ca2+-free alpha-amylase was binding to 10 Ca2+. All the results indicated that the dependence of enzyme conformation on Ca2+ was low.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 06:19:30