Abstract
Thioredoxin is a small (M, 12 000) protein con- taining an oxidation-reduction active cystine disulfide bridge [ 11, that has been ascribed several functions. The reduced form, thioredoxin-(SH)z, generated by NADPH and thioredoxin reductase, was the first isolated, in vitro hydrogen donor of ribonucleotide reductase [2]. It is also a general protein disulfide reductase; furthermore thioredoxin is an essential subunit of phage T7 DNA polymerase [3,4]. Glutaredoxin is another small acidic (M, 12 000) protein originally discovered in an
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