Khazaeli M B, Mitra R S
Appl Environ Microbiol. 1981 Jan;41(1):46-50. doi: 10.1128/aem.41.1.46-50.1981.
An inducible cadmium-binding protein was isolated from Escherichia coli cells accommodated to 3 X 10(-6) M Cd2+ but not from normal or unaccommodated cells. Sephadex G-100, metal chelate affinity chromatography, and disc gel electrophoresis were used in the purification procedure. The molecular weight of the Cd2+-binding protein was estimated to be about 39,000 by Sephadex G-100 chromatography, making it different from the conventional, much smaller metallothionein.
一种可诱导的镉结合蛋白是从适应于3×10⁻⁶ M Cd²⁺ 的大肠杆菌细胞中分离得到的，而在正常或未适应的细胞中则未分离到。在纯化过程中使用了葡聚糖凝胶G - 100、金属螯合亲和层析和圆盘凝胶电泳。通过葡聚糖凝胶G - 100层析估计，镉结合蛋白的分子量约为39000，这使其不同于传统的、小得多的金属硫蛋白。
