Purification and Characterization of α-L-Rhamnosidase from Bacteroides JY-6,a Human Intestinal Bacterium
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概要
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An α-L-rhamnosidase (EC 3.2.1.40) was purified 1500-fold from Bacteroides JY-6,an intestinal anaerobic bacterium of human. The specific activity of purified enzyme was 89.9 μmol/min/mg protein. The enzyme (M.W.240000) is composed of two subunits of M.W. 120000 with pI and optimal pH values of 4.2 and 7.0,respectively.The apparent K_<ms> for naringin, rutin and p-nitrophenyl-α-L-rhamnopyranoside were determined to be 0.89,1.44 and 0.29 mM, respectively. The enzyme was strongly inhibited by L-rhamnose, L-fucose, saccharic acid 1,4-lactone, p-chlormercuriphenylsulfonic acid and Pb^<2+>.
- 公益社団法人日本薬学会の論文
- 1996-12-15
著者
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Kim Dong-hyun
College Of Pharmacy Kyung Hee University
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JANG Il-Sung
College of Pharmacy Kyung Hee University
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Jang Il-sung
College Of Pharmacy Kyung-hee University
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Kim Do-hoon
Department Of Psychiatry College Of Medicine Institute Of Natural Medicine Hallym University
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Kim D‐h
Department Of Psychiatry College Of Medicine Institute Of Natural Medicine Hallym University
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Kim Dong-hyun
College Of Pharmacy
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