Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Flavobacterium meningosepticum 기원 Peroxidase의 정제 및 특성

  • 최양문 (고려대학교 생물공학연구소) ;
  • 조홍연 (고려대학교 생명공학원 및 연세대학교 생물산업소재연구센터) ;
  • 양한철 (고려대학교 생명공학원)
  • Published : 1996.10.01
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Abstract

Peroxidase was purified to homogeneity from cell free extract of Flavobacterium meningosepticum. The molecular weight of the enzyme estimated by gel filtration column chromatography was 220, 000. A identical subunit (54, 000) was detected on SDS-PAGE of the enzyme. From these results, the enzyme was supposed to have four identical subunits. On the basis of the visible absorption spectra of the purified enzyme, the enzyme was a typical hemoprotein. The isoelectric point of the enzyme was 4.1. On using N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m- toluidine (Toos) as a hydrogen donor, the enzyme showed optimum activity at the pH 5.5 and 50$\circ$C. The enzyme activity was inhibited by carbonyl reagent and Hg$^{2+}$ .

Keywords

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