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蓝藻金属硫蛋白的生理和化学特性

Physiological and chemical characterization of cyanobacterial metallothioneins.

作者信息

Olafson R W

出版信息

Environ Health Perspect. 1986 Mar;65:71-5. doi: 10.1289/ehp.866571.

DOI:10.1289/ehp.866571
PMID:3086079
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1474674/
Abstract

Techniques have been developed for detection, quantitation, and isolation of bacterial metallothioneins (MTs) from cyanobacterial species. These methods involve differential pulse polarography and reverse-phase high-performance liquid chromatography (HPLC) and have allowed detection of picomole quantities of these high sulfhydryl content proteins. The prokaryotic molecule was found to be induced in the presence of Cd or Zn salts with regulation at the level of transcription. Cu was not found to induce synthesis of the prokaryotic MT. Exposure to the former metals resulted in a growth lag followed by simultaneous induction of MT synthesis and onset of growth. Amino acid analysis and N-terminal sequence analysis indicated that the bacterial MTs from cyanobacteria are unique, having many aromatic and aliphatic residues and no apparent association of hydroxylated or basic amino acids with cysteines. Although the characteristic Cys-X-Cys sequences were present, no apparent amino acid sequence homology with the eukaryotic MTs was found in the first 42 residues.

摘要

已经开发出从蓝藻物种中检测、定量和分离细菌金属硫蛋白(MTs)的技术。这些方法包括差分脉冲极谱法和反相高效液相色谱法(HPLC),并且能够检测出皮摩尔量的这些高巯基含量的蛋白质。发现原核分子在镉盐或锌盐存在下被诱导,且在转录水平受到调控。未发现铜能诱导原核MT的合成。暴露于前一种金属会导致生长延迟,随后MT合成同时被诱导且生长开始。氨基酸分析和N端序列分析表明,来自蓝藻的细菌MT是独特的,具有许多芳香族和脂肪族残基,并且羟基化或碱性氨基酸与半胱氨酸之间没有明显的关联。尽管存在特征性的Cys-X-Cys序列,但在前42个残基中未发现与真核MT有明显的氨基酸序列同源性。

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本文引用的文献

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