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J Agric Food Chem ; 54(26): 9888-94, 2006 Dec 27.
Artículo en Inglés | MEDLINE | ID: mdl-17177516

RESUMEN

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.


Asunto(s)
Arecaceae/enzimología , Peroxidasa/aislamiento & purificación , Peroxidasa/metabolismo , Secuencia de Aminoácidos , Calcio/análisis , Estabilidad de Enzimas , Peróxido de Hidrógeno/metabolismo , Punto Isoeléctrico , Datos de Secuencia Molecular , Peso Molecular , Peroxidasa/química , Hojas de la Planta/enzimología , Especificidad por Sustrato
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