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KMID : 0376219730100010173
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Chonnam Medical Journal
1973 Volume.10 No. 1 p.173 ~ p.180
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Adenosine Diphosphate Ribose Pyrophosphohydrolase in Nasal Polyps
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Abstract
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Adenosine diphosphate ribose (ADPR) pyrophosphohydrolase, which catalyzes the hydrolysis at the pyrophosphate linkage of ADPR formed from NAD by NAD glycohydrolase to yield AMP and ribose-5´-phosphate, was assayed in nasal polyps together with NAD glycohydrolase. And some properties of the ADPR pyrophosphohydrolase were studied.
The activities of both ADPR pyrophosphohydrolase and NAD glycohydrolase were found to be high in nasal polyps, the former being more active than the latter.
The ADPR pyrophosphohydrolase of nasal polyps showed optimal pH around, 9.5. Although the crude enzyme did not require Mg2+ for its activity, the activity increased slightly, in the presence of 2.5 mM MgCl2. The enzyme was relatively heat-stable up to 60°, but completely inactivated by heat-treatment atDP, AMP and ATP, ADP being most inhibitory.
These results indicate that the enzyme ADPR pyrophosphohydrolase is ubiquitous being present not only in normal tissues but also in abnormal tissue such as nasal polyps. It is also suggested that the properties of the enzyme are tissuedependent.
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