One-step purification of an avocado peroxidase

Tipo de material: Texto

TextoSeries ; Plant Physiology and BioChemistry, 33(5), p.531-537, 1995Trabajos contenidos:

Sanchez Romero, C
Garcia Gomez, L
Pliego Alfaro, F
Heredia, A

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Resumen: A rapid isolati on procedure was developed for purification of a soluble ani onic isoperoxidase (donor: hydrogen peroxide oxidoreductase, EC 1.11.1.7)from avocado (Persea all1ericana, M. cv. Topa Topa)leaves. Electroelution from a native polyacrylamide gel, was the only requirement to achieve this. The purified isoperox idase was a monomer, 60 illa molecular mass, with a carbohydrate moiety. The amino acid composition showed 358 amino acid residues and appeared to be similar to those reported in other plant peroxidases. The study of some enzymatic properties, e. g. substrate specificity, susceptibility to effectors and so on, revealed that this isoperoxidase follows, in general, the action patterns previously established for anionic isoperoxidases.

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A rapid isolati on procedure was developed for purification of a soluble ani onic isoperoxidase (donor: hydrogen peroxide oxidoreductase, EC 1.11.1.7)from avocado (Persea all1ericana, M. cv. Topa Topa)leaves. Electroelution from a native polyacrylamide gel, was the only requirement to achieve this. The purified isoperox idase was a monomer, 60 illa molecular mass, with a carbohydrate moiety. The amino acid composition showed 358 amino acid residues and appeared to be similar to those reported in other plant peroxidases. The study of some enzymatic properties, e. g. substrate specificity, susceptibility to effectors and so on, revealed that this isoperoxidase follows, in general, the action patterns previously established for anionic isoperoxidases.

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