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A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor
Author(s) -
Trümper Susanne,
Follmann Hartmut,
Häberlein Ingo
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00947-3
Subject(s) - spinach , chloroplast , biochemistry , trypsin , homologous chromosome , chemistry , reductase , trypsin inhibitor , enzyme , botany , biology , gene
Dehydroascorbate reductase has been isolated from spinach chloroplasts and purified to apparent homogeneity. The N‐terminal amino acid sequence of the enzyme is homologous to the Kunitz‐type trypsin inhibitors from plant sources. It is shown that spinach DHA reductase and soybean trypsin inhibitor are both capable of reducing dehydroascorbate when in the reduced (thiol) form but acquire trypsin‐inhibiting activity in the oxidized (disulfide) state. Reduced chloroplast thioredoxins also reduce dehydroascorbate.