期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1980
卷号：77
期号：11
页码：6334-6338
DOI：10.1073/pnas.77.11.6334
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The reactions of Zn-, Zn,Cd-, and Cd-thioneins with EDTA and apo-carbonic anhydrase have been studied. The ligand substitution reaction of zinc with EDTA is multiphasic, having both associative and dissociative components in the rate expression. The cadmium sites are about 2 orders of magnitude less reactive. In contrast, apo-carbonic anhydrase abstracts zinc from Zn-thionein and Zn,Cd-thionein in second-order processes that are 2-3 orders of magnitude more rapid than those involving EDTA and approach the rate for unligated Zn2+ with the apo-protein. In comparison with other zinc proteins, Zn-thionein contains unusually reactive metal sites, suggesting that this protein may be a physiological zinc transfer protein, able to donate zinc to zinc-requiring apo macromolecules.
