Inactivation Study of Pyridine-Linked Dehydrogenases by $N^1$-Alkylnicotinamide Chlorides

$N^1$-Alkylnicotinamide Chloride 유도체에 의한 탈수소 효소의 불활성화에 관한 연구

  • 김수자 (수도여자사범대학 과학교육과) ;
  • 이현재 (한국과학원 생물공학과)
  • Published : 1976.10.30

Abstract

A series of $N^1$-alkylnicotinamide chlorides, $N^1$-methyl-to $N^1$-dodecylnicotinamides inclusive were studied with rabbit muscle L-${\alpha}$-glycerophosphate dehydrogenase to investigate the possibility of reversible and irreversible inactivation of the pyridine-linked dehydrogenases by the coenzyme-competitive inhibitor derivatives. The inhibition of the enzyme by $N^1$-alkylnicotinamide chlorides was demonstrated to be reversible at the dilute concentration of the inhibitors but this reversible inhibition was found to be followed by an irreversible time-dependent inactivation measuable at high concentrations of the inhibitors. The properties of this time-dependent inactivation were discussed on the basis of the denaturation of the enzyme by the binding of small micelle-like structures formed at higher concentrations of the inhibitors.

Pyridine관여 탈수소 효소는 $N^1$-alkylnicotinamide chloride 유도체에 의하여 저해 작용을 받고 있는 바 저해제이 농도 변화에 따른 효소 저해작용이 가역 또는 비가역 불활성화 반응에 기인하는지의 여부를 밝혀 보기 위하여 토끼 근육으로 부터 유리한 L-${\alpha}$-glycerophosphate dehydrogenase를 사용하여 연구하였다. 이 효소의 저해작용은 상용한 저해제 유도체의 농도가 희박했을 경우 가역적인 효소저해 반응을 보여주고 있으나 저해제의 농도가 증가함에 따라 점차 비가역적인 효소 불활성화로서 나타남을 알았으며 이러한 비가역 불활성화 반응은 저해제의 농도가 증가함에 따라 형성될 수 있는 micelle 구조의 미세분자와의 결합에 의한 효소의 변성에 기인할 것이라고 결론을 얻었다.

Keywords

References

  1. Biochim. Biophys Acta v.96 B.M. Anderosn;M.L. Reyolds
  2. Arch. Biochem. Biophys. v.111 no.1 B.M. Anderson;M.L. Reynolds
  3. J. Biol. Chem. v.243 S.J. Kim;B.M Anderson
  4. J. Biol. Chem. v.244 S.J. Kim;B.M. Anderson
  5. Arch. Biochem. Biophys. v.120 M.L. Fonda;B.M. Anderson
  6. Arch. Biochem. Biophys. v.106 T. Yonetani;H. Theorell
  7. Biochem. Z. v.329 K. Wellenfels;H. Sund;A. Dickmann
  8. J. Biol. Chem. v.241 B.M. Anderson.M.L. Reynolds
  9. Biochim. et Biophys Acta v.99 B.M. Anderson;M.L. Reynolds;C.D. Anderson
  10. J. Biol. Chem. v.244 S.J. Kim;B.M. Anderson
  11. Biochim. et Biophys. Acta v.67 W.W. Cleland
  12. Biochemistry v.1 H.R. Mahler;R.H. Baker;V.J. Schurer
  13. J. Phys. Chem. v.67 P. Mukerjee;A. Ray
  14. J. Colloid Sci. v.6 W.D. Harkins;H. Krizek;M.L. Corrin
  15. J. Colloid Interface Sci. v.21 W.P.J. Ford;R.H. Ottewill;H.C. Parreria
  16. Kolloid Z. v.96 J. Staff
  17. Z. Angew. Chem. v.80 P. Ekwall
  18. Kolloid Z. v.92 P. Ekwall
  19. Kinetics and Thermodynamics in Biochemistry H.G. Bray;K. White