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赤血球의 Adenosine Diphosphate Ribose Pyrophosphohydrolase

Adenosine Diphosphate Ribose Pyrophosphohydrolase from Rabbit Erythrocytes

전남의대잡지 1970년 7권 2호 p.159 ~ 168
은?基,
소속 상세정보
은?基 (  ) - 전남대학교 의과대학 생화학교실

Abstract


A soluble enzyme has been isolated and partially purified from rabbit erythrocytes which catalyzes the hydrolysis of adenosine diphosphate-5´-ribose (ADP-5´-ribose) to yield AMP and ribose-5´ phosphate:
ADP-5´-ribose+H_(2)O→AMP+Ribose-5´-phosphate
This enzyme shows optimal pH around 9.5 and requires Mg^(2+) and phosphate for the activity, the maximal activity being attained at 5 mM MgCI_(2) and 20 mM phosphate, It is heat-labile, being completely inactivated by heat-treatment at 60℃ for 10 minutes. The inactivation occurs even during storage at 4˚ of the purified enzyme but can be prevented by the presence of 5 mM MgCl_(2)
The enzyme is highly specific for ADP-5´-ribose as substrate and does not attack the pyrophosphate bonds of NAD, ATP and inorganic pyrophosphate. The apparent Michaelis constant for ADP-5´-ribose is 0.57mM.
A potent inhibitor of the enzyme is ADP which acts as a competitive inhibitor. Adenosine mono and triphosphate, inorganic pyrophosphate, oxidized and reduced NAD, and ribose-5´-phosphate are almost not inhibitory.
Since the enzyme can be widely detected in the erythrocytes, spleen, kidney, liver, brain, and muscle, it is suggested that the enzyme may play an important role in metabolic controls of NAD and ADP as well as of ADP-5´-ribose.

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