Zhao Y J, Sulkowski E, Porath J
Institute of Microbiology, Academia Sinica, Beijing, China.
Eur J Biochem. 1991 Dec 18;202(3):1115-9. doi: 10.1111/j.1432-1033.1991.tb16478.x.
Several avian and mammalian c-type lysozymes were chromatographed on chelated (to iminodiacetate) and immobilized transition metal ions (Co2+, Ni2+, Cu2+ and Zn2+) under a variety of experimental conditions. The varied affinity of evolutionary variants of the lysozyme family for chelated metal ions, IDA-M(II), can be rationalized primarily in terms of the presence, multiplicity and microenvironments of histidine residues. The chromatographic resolution of some of these closely related proteins attests to the analytical power of immobilized metal-ion affinity chromatography.
在多种实验条件下，对几种鸟类和哺乳动物的c型溶菌酶进行了螯合（亚氨基二乙酸）和固定化过渡金属离子（Co2+、Ni2+、Cu2+和Zn2+）色谱分析。溶菌酶家族进化变体对螯合金属离子IDA-M(II)的不同亲和力，主要可以根据组氨酸残基的存在、数量和微环境来解释。这些密切相关蛋白质中的一些在色谱上的分离证明了固定化金属离子亲和色谱的分析能力。
