Peroxidase from euphorbia characias latex: purification and properties |
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Authors: | Giovanni Floris Rosaria Medda Augusto Rinaldi |
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Institution: | Institute of Biological Chemistry, University of Cagliari, via Della Pineta 77, 09100 Cagliari, Italy |
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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. |
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Keywords: | Euphorbiaceae peroxidase hydrogen peroxide hemoproteins |
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