Calcium-related properties of horseradish peroxidase

Calcium-related properties of horseradish peroxidase

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 i...

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Veröffentlicht in:Biochemical and biophysical research communications 1978-02, Vol.80 (4), p.1039-1042
Hauptverfasser: Haschke, Richard H., Friedhoff, Jacqueline M.
Format: Artikel
Sprache:eng
Schlagworte:
Calcium - pharmacology
Edetic Acid
Guanidines
Horseradish Peroxidase - metabolism
Isoenzymes - metabolism
Kinetics
Peroxidases - metabolism
Protein Binding
Protein Conformation
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Zusammenfassung: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(78)91350-5