Identification and localization of the first glutaredoxin in leaves of a higher plant.
Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).
Morell
S
S
University of Kassel, Department of Biochemistry, Germany.
Follmann
H
H
Häberlein
I
I
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism; D002736:Chloroplasts / Q000201:enzymology; D003429:Cross Reactions; D004791:Enzyme Inhibitors / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D054477:Glutaredoxins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010088:Oxidoreductases / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D018515:Plant Leaves / Q000201:enzymology; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D011490:Protein Disulfide Reductase (Glutathione); D011506:Proteins / Q000276:immunology / Q000378:metabolism; D018724:Spinacia oleracea / Q000201:enzymology*; D014361:Trypsin Inhibitors; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D054477:Glutaredoxins; D010940:Plant Proteins; D011506:Proteins; D014361:Trypsin Inhibitors; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione); D000516:alpha-Amylases