STUDIES ON THE VARIOUS REFOLDED INTERMEDI ATES OF ALPHA-AMYLASE DENATURED BY UREA WITH HIGH-PERFORMANCE HYDROPHOBIC INTERACTION CHROMATOGRAPHY

Authors
BAI QA WEI YM GENG MH GENG XD
Citation
Qa. Bai et al., STUDIES ON THE VARIOUS REFOLDED INTERMEDI ATES OF ALPHA-AMYLASE DENATURED BY UREA WITH HIGH-PERFORMANCE HYDROPHOBIC INTERACTION CHROMATOGRAPHY, Gaodeng xuexiao huaxue xuebao, 18(8), 1997, pp. 1291-1295
Citations number
7
Categorie Soggetti
Chemistry
Journal title
Gaodeng xuexiao huaxue xuebao → ACNP
ISSN journal
02510790
Volume
18
Issue
8
Year of publication
1997
Pages
1291 - 1295
Database
ISI
SICI code
0251-0790(1997)18:8<1291:SOTVRI>2.0.ZU;2-S
Abstract
alpha-Amylase originally denatured with 8.0 mol/L urea and its refolde d intermediates were investigated by high performance hydrophobic inte raction chromatography. Many kinds(at least 19) of its refolded interm ediates were obtained and found to be relatively stable, at least for a week, in their respective solutions of the mobile phase used. The re sult was further proved by the methods of electrophoresis, ion exchang e chromatography and size exclusive chromatography. In addition, the d ifference between the molecular conformations of these intermediates w as investigated by ultraviolet-absorption spectrum and fluorescence em ission spectrum.