活化的人中性粒细胞蛋白质中蛋氨酸残基的氧化
Oxidation of methionine residues in proteins of activated human neutrophils.
作者信息
Fliss H, Weissbach H, Brot N
出版信息
Proc Natl Acad Sci U S A. 1983 Dec;80(23):7160-4. doi: 10.1073/pnas.80.23.7160.
A simple assay for the detection of 35S-labeled methionine sulfoxide residues in proteins is described. The assay, which is based on the ability of CNBr to react with methionine but not with methionine sulfoxide, requires the prelabeling of cellular proteins with [35S]methionine. The assay was used to study the extent of methionine oxidation in newly synthesized proteins of both activated and quiescent human neutrophils. In cells undergoing a phorbol 12-myristate 13-acetate-induced respiratory burst, about 66% of all methionine residues in newly synthesized proteins were oxidized to the sulfoxide derivative, as compared with 9% in cells not treated with the phorbol ester. In contrast, quantitation of methionine sulfoxide content in the total cellular protein by means of amino acid analysis showed that only 22% of all methionine residues were oxidized in activated cells as compared with 9% in quiescent cells. It is proposed that methionine residues in nascent polypeptide chains are more susceptible to oxidation than those in completed proteins.
本文描述了一种用于检测蛋白质中35S标记的甲硫氨酸亚砜残基的简单测定方法。该测定方法基于溴化氰与甲硫氨酸反应但不与甲硫氨酸亚砜反应的能力，需要用[35S]甲硫氨酸对细胞蛋白质进行预标记。该测定方法用于研究活化和静止的人类中性粒细胞新合成蛋白质中甲硫氨酸氧化的程度。在经历佛波醇12-肉豆蔻酸酯13-乙酸酯诱导的呼吸爆发的细胞中，新合成蛋白质中约66%的甲硫氨酸残基被氧化为亚砜衍生物；相比之下，未用佛波醇酯处理的细胞中这一比例为9%。相反，通过氨基酸分析对总细胞蛋白中甲硫氨酸亚砜含量进行定量分析表明，活化细胞中所有甲硫氨酸残基只有22%被氧化，而静止细胞中这一比例为9%。有人提出，新生多肽链中的甲硫氨酸残基比完整蛋白质中的甲硫氨酸残基更容易被氧化。
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