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4 . Adenosine Diphosphate Ribose Pyrophosphatase from Rabbit Erythrocytes
이강만,이민화,김형로 생화학분자생물학회 1973 BMB Reports Vol.3 No.1
A soluble enzyme has been isoated and partially purified from rabbit erythrocytes which catalyzes the hydrolysis of pyrophosphate bond of adenosine diphosphate-5'-ribose (ADP-5'ribose) to yield ribose-5'-phosphate and AMP: ADP-5'-ribose+H₂O → Ribose-5'-phosphate+AMP The enzyme shows optimal pH around 9.5 and requires Mg^(++) and inorganic phosphate for the maximal activity. It is heat-labile, and the inactivation during storage at 4 of the purified enzyme can be prevented by Mg^(++). The enzyme is highly specific for ADP-5'-ribose as substrate and does not attack pyrophosphate bonds of NAD, ATP and inorganic pyrophosphate. The apparent Michaelis constant for ADP-5'-ribose is 0.5 mM.
Effect of Adenosine Diphosphate Ribose on Platelet Aggregation
이강만,이민화,김형로 생화학분자생물학회 1974 BMB Reports Vol.3 No.2
Adenosine diphospate-5'-ribose (ADP-ribose), which is produced from NAD by the action of NAD nucleosidase, has dual effect on platelet aggregation in citrated platelet-rich rabbit plasma at concentrations more than 1 × 10^(-4) M, it induces platelet aggregation immediately on the one hand, and on the other hand it inhibits platelet aggregation induced by ADP and by collagen after the platelet that had aggregated in the presence of ADP-ribose dispersed again after a few minutes. Since the enzyme ADP-ribose pyrophosphohydrolase, which catalyzes the hydrolysis of ADPribose to AMP and ribose-5'-phosphate, could be identified in platelet-free plasma, it appears likely that the inhibitory effect of ADP-ribose on platelet-aggregation induced by ADP or collagen is due to AMP which is enzymatically produced from ADP-ribose in platelet-rich plasma.