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大鼠肝脏铜金属硫蛋白的代谢研究。

Studies on the metabolism of rat liver copper-metallothionein.

作者信息

Mehra R K, Bremner I

出版信息

Biochem J. 1985 May 1;227(3):903-8. doi: 10.1042/bj2270903.

Abstract

The degradation of purified 35S-labelled rat liver isometallothioneins (MT) by lysosomal extracts was studied. Zn-MT-I was more readily hydrolysed than Zn-MT-II, but no significant degradation of the Cu-containing metallothioneins could be detected, even after 24 h incubation. The susceptibility of MT to degradation in vitro may be related to the strength of the metal-thiolate bonds. However, the turnover rates of cytosolic MT in vivo, as established by pulse-labelling techniques, are apparently subject to different controls. The half-lives of MT-I and -II in the liver cytosol of Cu2+-injected rats were only 15.4 +/- 1.5 and 18.2 +/- 1.1 h respectively. Approx. 25% of the total liver MT was present in particulate fractions (probably in lysosomes) of the liver and had a half-life of 25.1 +/- 4.1 h.

摘要

研究了溶酶体提取物对纯化的35S标记大鼠肝脏异金属硫蛋白(MT)的降解作用。锌-金属硫蛋白-I比锌-金属硫蛋白-II更容易被水解,但即使孵育24小时后,也未检测到含铜金属硫蛋白有明显降解。MT在体外的降解敏感性可能与金属硫醇盐键的强度有关。然而,通过脉冲标记技术确定的体内胞质MT的周转率显然受到不同的调控。注射铜离子的大鼠肝脏胞质中金属硫蛋白-I和-II的半衰期分别仅为15.4±1.5小时和18.2±1.1小时。肝脏中约25%的总MT存在于肝脏的颗粒部分(可能在溶酶体中),其半衰期为25.1±4.1小时。

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Differences in the polymorphic forms of metallothionein.金属硫蛋白多态形式的差异。
Arch Biochem Biophys. 1982 Mar;214(1):80-8. doi: 10.1016/0003-9861(82)90010-8.

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