Reference: Gan ZR, et al. (1990) Complete amino acid sequence of yeast thioltransferase (glutaredoxin). Biochem Biophys Res Commun 168(3):944-51

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Abstract


The amino acid sequence of a thioltransferase isolated from Saccharomyces cerevisiae was determined. The protein was cleaved by trypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The peptides generated were purified by reverse phase HPLC. Sequencing of intact protein and its fragments were achieved by automated Edman degradation. The protein contains 106 amino acid residues with two cysteines. Yeast thioltransferase showed 51% structural similarity to pig liver thioltransferase and 34% to E. coli glutaredoxin.

Reference Type
Comparative Study | Journal Article
Authors
Gan ZR, Polokoff MA, Jacobs JW, Sardana MK
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