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Comparative Study
. 1990 May 16;168(3):944-51.
doi: 10.1016/0006-291x(90)91120-h.

Complete amino acid sequence of yeast thioltransferase (glutaredoxin)

Z R Gan  1 , M A Polokoff, J W Jacobs, M K Sardana
Affiliations
Comparative Study

Complete amino acid sequence of yeast thioltransferase (glutaredoxin)

Z R Gan et al. Biochem Biophys Res Commun. .

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.

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