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KMID : 0357319960310050547
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Journal of the Korean Society for Microbiology
1996 Volume.31 No. 5 p.547 ~ p.556
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Purification and Ccharacterization of Helicobacter pylori Alcohol Dehydrogenase(ADH)
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조명제
이우곤/최여정/안영숙/류복덕/윤영혜/백승철/전영석/이과오
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Abstract
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Hlicobacter pylori cytosol was chromatographed on a Sephacry1 S200 column and on Cibacron blus 3GA ligand in order to get a purified alcohol dehydrogenase (ADH). Size estimations by SDS-denaturing polyacrylamide gel electorphoresis and by gel
fitration
revealed that Helicobacter pylori ADH was a monomer of 40.6 kDa protein. The Kms of Helicobacter pylori ADH for NADP and NAD reduction were 0.08 mM and 0.52 mM/L, respectively. And the Km of Helicobacter pylori ADH for ethanol oxidation was
18.2mM.
The
Helicobacter pylori ADH didn't show any NAD or NADP-linked acetaldehyde dehydrogenase activity and was competitively inhibited by 4-methy1pyrazole. Optimal pH and temperature of Helicobacter pylori ADH were 9.4 and 25℃, respectively. These
results
implicated that Helicobacter pylori ADH is supposed to form acetaldehyde adducts in the tissue when ethanol is endogenously and exogenously added to gastroduodenal mucosa, implying Helicobacter pylori ADH may partly contribute to gastroduodenal
damage
associated with Helicobacter pylori infection.
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KEYWORD
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