PMID: 11322884Apr 27, 2001Paper

Purification and characterization of acharan sulfate lyases, two novel heparinases, from Bacteroides stercoris HJ-15

European Journal of Biochemistry
B T KimD H Kim

Abstract

Two novel acharan sulfate lyases (ASL1 and ASL2: no EC number) have been purified from Bacteroides stercoris HJ-15 which was isolated from human intestinal bacteria with glycosaminoglycan (GAG) degrading enzymes. These enzymes were purified to apparent homogeneity by a combination of QAE-cellulose, DEAE-cellulose, carboxymethyl-Sephadex C-50, hydroxyapatite and HiTrap SP Sephadex C-25 column chromatography with the final specific activity of 50.5 and 76.7 micromol.min-1.mg-1, respectively. Both acharan sulfate lyases are single subunits of 83 kDa by SDS/PAGE and gel filtration. ASL1 showed optimal activity at pH 7.2 and 45 degrees C. ASL1 activity was inhibited by Cu2+, Ni2+ and Co2+, but ASL2 activity was inhibited by Cu2+, Ni2+and Pb2. Both enzymes were slightly inhibited by some agents that modify histidine and cysteine residues, but activated by reducing agents such as DL-dithiothreitol and 2-mercaptoethanol. Both purified bacteroidal acharan sulfate lyases acted to the greatest extent on acharan sulfate, and to a lesser extents on heparan sulfate and heparin. They did not act on de-O-sulfated acharan sulfate. These findings suggest that the biochemical properties of these purified acharan sulfate lyases are different from ...Continue Reading

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Citations

Nov 3, 2001·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·J JeongY S Kim
Jul 19, 2003·European Journal of Biochemistry·Sung-Woon HongDong-Hyun Kim
Dec 21, 2004·Journal of Biochemistry and Molecular Biology·Wan-Seok KimYeong Shik Kim
Jan 30, 2008·Protein Expression and Purification·Kyu-Woong Shim, Dong-Hyun Kim
Jul 1, 2004·Critical Reviews in Biotechnology·P MichaudJ Courtois

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