TY  - BOOK
AU  - Haschke,R.H.
AU  - Friedhoff,J.M.
TI  - Calcium-related properties of horseradish peroxidase
N2  - Horseradish 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
UR  - https://drive.google.com/file/d/19D4oIRSBP63pboCnrueTysSz6feimxhr/view?usp=drivesdk
ER  -