Human recombinant CuZn-superoxide dismutase. Amino acid sequence and location of the disulfide bond.

M Peretz, M U Werber, Y Burstein
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Abstract

The complete amino acid sequence of recombinant human Cu-Zn superoxide dismutase (CuZnSOD) is presented. The S-carboxymethylated protein was cleaved at lysine residues (with Achromobacter protease I) to provide a set of nine non-overlapping fragments accounting for 90% of the sequence. These fragments were then overlapped and aligned, and the sequence was completed by using peptides generated by cleavage at glutamic acid residues (with S. aureus V8 protease) and at arginine (with clostripain). The recombinant protein contains a single disulfide bond between cysteine residues 57 and 146. The primary sequence of recombinant human CuZnSOD is identical to that predicted by its cDNA sequence.

人重组cuzn -超氧化物歧化酶。二硫键的氨基酸序列和位置。
获得了重组人铜锌超氧化物歧化酶(CuZnSOD)的完整氨基酸序列。s -羧甲基化蛋白在赖氨酸残基处被切割(用无色杆菌蛋白酶I),得到一组9个不重叠的片段,占序列的90%。然后将这些片段重叠并对齐,利用谷氨酸残基(用金黄色葡萄球菌V8蛋白酶)和精氨酸残基(用clostripain)裂解产生的肽段完成序列。重组蛋白在半胱氨酸残基57和146之间含有一个单二硫键。重组人CuZnSOD的原序列与cDNA序列预测的原序列一致。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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