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090			_aB-17163
245	1	0	_aOne-step purification of an avocado peroxidase
490	0		_vPlant Physiology and BioChemistry, 33(5), p.531-537, 1995
520	3		_aA 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.
650	1	4	_aTSOPEROXIDASE
650	1	4	_aISOLATION
650	1	4	_aPERSEA AMERICANA
700	1	2	_aSanchez Romero, C.
700	1	2	_aGarcia Gomez, L.
700	1	2	_aPliego Alfaro, F.
700	1	2	_aHeredia, A.
856	4	0	_uhttps://drive.google.com/file/d/1GNE6-bMeXIQbEh3ZH8UmlHG2JiNpaUww/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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