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  • Title: Purification and characterization of windmill palm tree (Trachycarpus fortunei) peroxidase.
    Author: Caramyshev AV, Firsova YN, Slastya EA, Tagaev AA, Potapenko NV, Lobakova ES, Pletjushkina OY, Sakharov IY.
    Journal: J Agric Food Chem; 2006 Dec 27; 54(26):9888-94. PubMed ID: 17177516.
    Abstract:
    High peroxidase activity was demonstrated to be present in the leaf of several species of cold-resistant palms. Histochemical studies of the leaf of windmill palm tree (Trachycarpus fortunei) showed the peroxidase activity to be localized in hypoderma, epidermis, cell walls, and conducting bundles. However, chlorophyll-containing mesophyll cells had no peroxidase at all. The leaf windmill palm tree peroxidase (WPTP) was purified to homogeneity and had a specific activity of 6230 units/mg, RZ = 3.0, a molecular mass of 50 kDa, and an isoelectric point of pI 3.5. The electronic spectrum of WPTP with a Soret band at 403 nm was typical of plant peroxidases. The N-terminal amino acid sequence of WPTP was determined. The substrate specificity of WPTP was distinct from that of other palm peroxidases, and the best substrate for WPTP was 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid). The palm peroxidase showed an unusually high stability at elevated temperatures and high concentrations of guanidine.
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