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245	1	0	_aCalcium-related properties of horseradish peroxidase
490	0		_vBioChemical and Biophysical Research Communications, 80, p.1039-1042, 1978
520	3		_aHorseradish peroxidase has been shown to be a metalloprotein in which calcium contributes to the structural stability of the protein. Isoenzyme C and A contain 2.0 and 1.4 moles calcium/mole enzyme, respectively, which can be removed by treatment with guanidine hydrochloride and EDTA. Calcium-free isoenzyme C, but not isoenzyme A, reconstitutes upon addition of calcium and regains enzymatic activity. Free calcium readily exchanges with isoenzyme C, but only to a small extent with isoenzyme A. In addition the role of calcium in maintaining molecular conformation is evidenced by the effects of calcium removal from the isoenzyme C on the thermal stability of the protein.
700	1	2	_aHaschke, R.H.
700	1	2	_aFriedhoff, J.M.
856	4	0	_uhttps://drive.google.com/file/d/19D4oIRSBP63pboCnrueTysSz6feimxhr/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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