Glutaredoxin(thioltransferase) has been identified and purified to hom
ogeneity from spinach leaves. Its cytosolic localization was demonstra
ted by chromatographic and immunological analysis of extracts from iso
lated spinach chloroplasts and mitochondria, respectively. Spinach glu
taredoxin shows a significant crossreactivity with antibodies raised a
gainst E. coli glutaredoxin and possesses a specific thioltransferase
activity comparable to that of the E. coli protein. Minor thioltransfe
rase activities (less than 10% of total leaf activity) have been obser
ved in spinach chloroplasts which are probably due to the presence of
trypsin inhibitor and thioredoxins (TRf and TRm).