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 → Rib...
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https://www.riss.kr/link?id=A3289667
1973
English
472
SCIE,SCOPUS,KCI등재
학술저널
3-3(1쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
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 → Rib...
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.
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