Intermediates in guanidine-HC1 unfolding of glutamine synthetase from the extreme thermophile, Bacillus caldolyticus.
作者信息
Wedler F C, McLean M A
机构信息
Department of Molecular and Cell Biology, Althouse Laboratory, Pennsylvania State University, University Park 16802.
出版信息
Biochim Biophys Acta. 1991 Jan 8;1076(1):161-3. doi: 10.1016/0167-4838(91)90235-r.
PMID:1670923
Abstract
Glutamine synthetase is expressed in Bacillus caldolyticus as two isoforms that differ in physico-chemical and regulatory properties. Biphasic kinetics of thermal denaturation of E-I and E-II (Merkler, D.J., et al (1987) Biochemistry 26, 7805), suggested the formation of intermediates. CD spectral changes of E-II induced by guanidine-HC1 clearly indicate a three-state pathway for unfolding (N----I----D). Refolding of E-II from 6 M GuHCl led to only 15% recovery of activity, compared to greater than or equal to 90% with E-I.
摘要
Zotero 插件