Flavobacterium meningosepticum이 생산하는 Nucleoside Oxidase의 효소학적 특성

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

Abstract

The molecular weight of the purified nucleoside oxidase estimated by gel filtration column chromatography was 480,000 and the enzyme protein was composed of four nonidentical subunits (81,000, 69,000, 32,000 and 16,000). On the basis of the visible absorption spectra and the enzymatic determination of the purified enzyme, the enzyme was supposed as a hemoprotein and also a flavoprotein containing 3 moles of FAD per I mole of enzyme. The isoelectric point of the enzyme was pH 5.1. Addition of metal salts such as 1 mM SnCl$_{2}$ and PbCl$_{2}$ into an enzyme reaction solution inhibited the enzyme activity by 94 and 90%, respectively. The enzyme activity was also lost significantly by hemoenzyme inhibitors such as NaCN and NaN$_{3}$ and flavoenzyme inhibitor, acriflavine and quinacrine. The maximal nucleoside oxidase activity was observed at pH 7.0 and 55$\circ$C. The nucleoside oxidase was relatively stable in the range of pH 5.5-9.0 and below 55$\circ$C.

Keywords

References

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