토끼 Hemoglobin 의 Peroxidase 활성에 관한 연구 = Studies on the Peroxidase Activity of Rabbit Hemoglobin

다국어 초록 (Multilingual Abstract)

Rabbit hemoglobin was purified by using ammonium sulfate fractionation, CM-Sephadex chromatography, hydroxyapatite chromatography and Sephadex G-100 gel filtration. The purified hemoglobin oxidized various synthetic and naturally occurring phenolic compounds in the presence of H₂O₂. The substrate specificity studies indicate that rabbit hemoglobin has about 10 times lower K_m values for guaiacol (0.39 mM) and o-dianisidine (0.09 mM) when compared to those of plant peroxidases. Among natural substrates tested, rabbit hemoglobin catalyzes the oxidation of caffeic acid, chlorogenic acid and indole-3-acetic acid quite rapidly compare to other naturally occurring phenolic compounds such as scopoletin, esculetin, ferulic acid and p-coumaric acid. In general, phenolic compounds having methoxy group appears to have high affinity to rabbit hemoglobin as revealed by their very low K_m values. Chemical modification studies indicate that p-chloromercuribenzoate inactivates the peroxidase activity of rabbit hemoglobin, whereas N-ethylmaleimide or iodoacetamide does not. Furthermore, the peroxidase activity of rabbit hemoglobin is rapidly inactivated by diethylpyrocarbonate, a histidyl selective reagent, unlike plant peroxidases.