Current time in Korea 19:17 Oct 27 (Tue) Year 2020 KCS KCS Publications
KCS Publications
My Journal  Log In  Register
HOME > Search > Browsing(JKCS) > Archives

Journal of the Korean Chemical Society (JKCS)

ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 20, Number 5
JKCSEZ 20(5)
October 20, 1976 

 
Title
Inactivation Study of Pyridine-Linked Dehydrogenases by N1-Alkylnicotinamide Chlorides

N1-Alkylnicotinamide Chloride 유도체에 의한 탈수소 효소의 불활성화에 관한 연구
Author
Soo Ja Kim, Hyun-Jae Lee

김수자, 이현재
Keywords
Abstract
Pyridine관여 탈수소 효소는 N'-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-α-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.

A series of N1-alkylnicotinamide chlorides, N1-methyl-to N1-dodecylnicotinamides inclusive were studied with rabbit muscle L-α-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 N1-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.

Page
406 - 416
Full Text
PDF