The isolation and primary structure of a peptide containing the oxidation-reduction active cystine of Escherichia coli thioredoxin reductase.
نویسندگان
چکیده
An octapeptide from Escherichia coli thioredoxin reductase has been isolated and sequenced; it contains the cystine previously shown to take part in electron transfer. The peptide was isolated from a peptic digest of a derivative in which the free sulfhydryls of the enzyme had been reacted with the colored maleimide, N-(4-dimethylamino-3 ,S-dinitrophenyl)maleimide. The sequence of this peptide as determined by subtractive Edman degradation was:
منابع مشابه
The amino acid sequence of a peptide containing the active center disulfide of thioredoxin reductase from Escherichia coli.
Thioredoxin is a low molecular weight protein. In the oxidized form, thioredoxin-S2, it contains a single disulfide bridge formed from the 2 half-cystine residues in the molecule (1). The reduced or dithiol form of thioredoxin, thioredoxin-(SH)z, was first identified as the hydrogen donor in the reduction of ribonucleotides to deoxyribonucleotides in Escherichia coli (2). It has now been shown ...
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Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/o...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 247 7 شماره
صفحات -
تاریخ انتشار 1972