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Horseradish Peroxidase Renaturation Is Less Efficient at Lower Protein Concentrations

[ Vol. 12 , Issue. 7 ]

Author(s):

D. N. Ermolenko, A. V. Zherdev and B. B. Dzantiev   Pages 639 - 643 ( 5 )

Abstract:


Renaturation of horseradish peroxidase from guainidine hydrochloride has been studied. Although refolding of the secondary structure was complete, only partial heme incorporation and recovery of enzymatic activity were observed. Heme capturing became less efficient at lower peroxidase concentrations: the refolding yield decreased from 60% at 1 μM to 10% at 0.1 μM concentration of the protein. Probing with conformation-sensitive antibodies indicated structural differences between peroxidase refolded at low concentration and the holo-enzyme.

Keywords:

horseradish peroxidase, apo-enzyme, Refolding, heme, guanidine hydrochloride

Affiliation:

Institute of Biochemistry,Russian Academy of Sciences, Leninsky prospect 33, 119071 Moscow,Russia;



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