TAILIEUCHUNG - Báo cáo Y học: Purification and characterization of novel chondroitin ABC and AC lyases from Bacteroides stercoris HJ-15, a human intestinal anaerobic bacterium

Two novel chondroitinases, chondroitin ABC lyase (EC ) and chondroitin AC lyase (EC ), have been purified from Bacteroides stercoris HJ-15, which was isolated from human intestinal bacteria with glycosaminoglycan degrading enzymes. Chondroitin ABC lyase was purified to apparent homogeneity by a combination of QAE-cellulose, CM-Sephadex C-50, hydroxyapatite and Sephacryl S-300 column chromatography with a final specific activity of lmolÆmin)1Æmg)1. Chondroitin AC lyase was purified to apparent homogeneity by a combination of QAE-cellulose, CM-Sephadex C-50, hydroxyapatite and phosphocellulose column chromatography with a final specific activity of lmolÆmin)1Æmg)1 | Eur. J. Biochem. 269 2934-2940 2002 FEBS 2002 doi Purification and characterization of novel chondroitin ABC and AC lyases from Bacteroides stercoris HJ-15 a human intestinal anaerobic bacterium Sung-Woon Hong1 Byung-Taek Kim1 Ho-Young Shin1 Wan-Suk Kim2 Keun-Sook Lee1 Yeong-Shik Kim2 and Dong-Hyun Kim1 1 College of Pharmacy Kyung Hee University Seoul Korea 2Natural Products Research Institute Seoul National University Seoul Korea Two novel chondroitinases chondroitin ABC lyase EC and chondroitin AC lyase EC have been purified from Bacteroides stercoris HJ-15 which was isolated from human intestinal bacteria with glycosaminoglycan degrading enzymes. Chondroitin ABC lyase was purified to apparent homogeneity by a combination of QAE-cellulose CM-Sephadex C-50 hydroxyapatite and Sephacryl S-300 column chromatography with a final specific activity of imol-min_1-mg_1. Chondroitin AC lyase was purified to apparent homogeneity by a combination of QAE-cellulose CM-Sephadex C-50 hydroxyapatite and phosphocellulose column chromatography with a final specific activity of pmol-min_1-mg_1. Chondroitin ABC lyase is a single subunit of 116 kDa by SDS PAGE and gel filtration. Chondroitin AC lyase is composed of two identical subunits of 84 kDa by SDS PAGE and gel filtration. Chondroitin ABC and AC lyases showed optimal activity at pH and 40 C and and 45-50 C respectively. Both chondroitin lyases were potently inhibited by Cu2 Zn2 and p-chloromercuriphenyl sulfonic acid. The purified Bacteroidal chondroitin ABC lyase acted to the greatest extent on chondroitin sulfate A chondroitin 4-sul-fate to a lesser extent on chondroitin sulfate B dermatan sulfate and C chondroitin 6-sulfate . The purified chondroitin AC lyase acted to the greatest extent on chondroitin sulfate A and to a lesser extent on chondroitin C and hyaluronic acid. They did not act on heparin and heparan sulfate. These findings suggest that the .

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