Paliwal V K, Kohli K K, Sharma M, Nath R
Mol Cell Biochem. 1986 Aug;71(2):139-47. doi: 10.1007/BF00214773.
Metallothionein (MT) a low molecular weight, Cd-binding, cysteine rich, cytosolic protein has been isolated, purified and characterized from cadmium exposed Rhesus monkeys maintained on protein calorie malnourished (PCM) diet. Metallothionein was resolved into three isoforms i.e. MTa, MTb and MTc. The ratio of Cd, Zn and Cu varied in these isometallothioneins. MTc was the major isometallothionein. U.V. Spectra of MTc revealed the presence of mercaptide bonds and absence of aromatic amino acids. These observations were further confirmed by amino acid analysis of MTc which demonstrated high cysteine content (22.6) followed by serine, glycine and lysine. The molecular weight of MTc as determined by gel filtration and amino acid analysis was 13,000 and 6398 daltons respectively. This demonstrates that MTc is a nonglobular ellipsoid polypeptide. MTc showed a unique property of binding selenium. Monkey liver metallothionein was immunologically identical with human metallothionein. All the characteristics of MTc obtained in the present study reveal a similarity between monkey and human metallothionein probably due to closer phylogenetic relationship between the two species.
金属硫蛋白（MT）是一种低分子量、能结合镉、富含半胱氨酸的胞质蛋白，已从以蛋白质热量营养不良（PCM）饮食维持的镉暴露恒河猴中分离、纯化并进行了表征。金属硫蛋白可分为三种亚型，即MTa、MTb和MTc。这些异金属硫蛋白中镉、锌和铜的比例各不相同。MTc是主要的异金属硫蛋白。MTc的紫外光谱显示存在硫醇键且不存在芳香族氨基酸。MTc的氨基酸分析进一步证实了这些观察结果，该分析表明半胱氨酸含量高（22.6），其次是丝氨酸、甘氨酸和赖氨酸。通过凝胶过滤和氨基酸分析测定的MTc分子量分别为13,000和6398道尔顿。这表明MTc是一种非球形的椭球状多肽。MTc表现出结合硒的独特特性。猴肝金属硫蛋白与人类金属硫蛋白在免疫上相同。本研究中获得的MTc的所有特征揭示了猴和人类金属硫蛋白之间的相似性，这可能是由于这两个物种之间更密切的系统发育关系。
