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KMID : 0380219930260020151
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 2 p.151 ~ p.156
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Essential Sulfhydryl Residue in Radish Peroxidase Isozyme
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Mi Joung Lee and Soung Soo Kim
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Abstract
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Purified isoperoxidase A1 from Korean radish (raphanus sativus L.) root was rapidly inactivated by the thiol specific reagent p-hydroxymercuribenzoate (PHMB) having minor polarity, but not by N-ethylmaleimide, isdoacetamide or 5,5'-dithiobis-(2-nitrobenzoate) at various concentrations of these reagents. The inhibitory effect was protected by substrate guaiacol and by preincubation the enzyme with orgainc solvent such s methanol and t-butanol, which decreased the inactivation was calculated to be 1.6×10E3M-1.min-1, and the reaction order with respect to PHMB was 1.15, indicaiting that there may be one essential sulfhydryl residuce per active enzyme.
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