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- W2054449802 abstract "A peroxidase has been purified to homogeneity from Euphorbia characias latex using ammonium sulfate precipitation and chromatography on DEAE-cellulose, hydroxylapatite and SP-Sephadex columns. The substrate specificity of the enzyme is typical of a plant peroxidase except that it shows no activity with indole-3-acetic acid. The pH optimum of the enzyme was 5.75 and the isoelectric point 7.4. The activation energy was 14 kcal/mol. The prosthetic group was shown to be ferriprotoporphyrin IX. Gel chromatography and PAGE indicate that the purified protein is composed of a single polypeptide chain having a MW of ca 48 000." @default.
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- W2054449802 date "1984-01-01" @default.
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- W2054449802 title "Peroxidase from euphorbia characias latex: purification and properties" @default.
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- W2054449802 doi "https://doi.org/10.1016/s0031-9422(00)82590-x" @default.
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