期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 465, 期 1, 页码 247-253出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.05.023
关键词
metallothionein; cadmium-binding; cadmium-release; copper-binding; structure-function relationship; circular dichroism; absorption spectroscopy; fluorescence emission spectroscopy; Mytilus galloprovincialis
Structure and function of molluscan metallothioneins (MTs) are still poorly understood. The sea mussel Mytilus galloprouincialis displays two MT isoforms which differ in both primary sequences and physiological functions. MT-10 is the constitutive isoform, whereas MT-20 is mainly induced by cadmium (Cd). Both MTs were produced as recombinant proteins and showed identical Cd content and similar Cd-binding properties. Conversely, circular dichroism disclosed marked differences in the secondary conformations of the two Cdr-MTs. The possible relapses of these structural differences on protein stability and function were assessed. MT-10 presented a higher thermal stability and a more compact structure than MT-20, as it was inferred by absorption and emission spectroscopy studies. Moreover, the kinetics of Cd-release clearly indicated that MT-10 is much more sensitive to oxidation than is MT-20. The observed differences between MT-10 and MT-20 are discussed in terms of the different physiological roles exerted by the two isoforms in mussel. (c) 2007 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据