Rapid Purification, Characterization and Substrate Specificity of Heparinase from a Novel Species of Sphingobacterium

Journal of Biochemistry

Volumn 134, Issue 3, 2003, Pages 365-371

  Yapeng, Chao ^a   Ningguo, Gao ^a   Xiulan, Cheng ^a   Jing, Yang ^a   Shijun, Qian ^a   Shuzheng, Zhang ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

Author keywords

Heparinase; Rapid purification; Sphingobacterium sp; Substrate specificity

Indexed keywords

BACTERIAL ENZYME; HEPARAN SULFATE; HEPARIN; HEPARIN DERIVATIVE; HEPARIN LYASE; N ACETYLHEPARIN; N ACETYLIMIDAZOLE; PEPTIDE; SEPHAROSE; TYROSINE; UNCLASSIFIED DRUG;

ACETYLATION; AMINO ACID COMPOSITION; ANALYTIC METHOD; ARTICLE; BACTERIAL STRAIN; BACTERIUM ISOLATION; BINDING SITE; CHROMATOGRAPHY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; ELECTRIC POTENTIAL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME INHIBITION; ENZYME ISOLATION; ENZYME MODIFICATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; FLAVOBACTERIUM; GRAM NEGATIVE BACTERIUM; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OSMOTIC STRESS; PROTEIN DATABASE; PROTEIN STRUCTURE; SPHINGOBACTERIUM; SULFATION; TECHNIQUE;

AMINO ACIDS; ANIMALS; CATTLE; HEPARIN LYASE; OSMOTIC PRESSURE; POLYSACCHARIDES; SPHINGOBACTERIUM; SUBSTRATE SPECIFICITY; SWINE;

BACTERIA (MICROORGANISMS); BOVINAE; FLAVOBACTERIUM; NEGIBACTERIA; SPHINGOBACTERIUM;

EID: 0142121657     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg154     Document Type: Article

References (22)

1. Casu, B. (1990) Heparin structure. Haemostasis 20 (suppl. 1), 62-73
2. Linhardt, R.J. (1996) Heparin and heparin oligosaccharides: preparation, analysis, application and biological activities in Biomedical Functions and Biotechnology of Natural and Artificial Polymers. (Yalpani, M., ed.) ATL Press
3. Linhardt, R.J., Wang, H.M., Loganathan, D., and Bae, J.H. (1992) Searching for the heparin antithrombin III-binding site precusor. J. Biol. Chem. 267, 2380-2387
4. Linhardt, R.J., Galliher, P.M., and Coony, C.L. (1986) Polysacharide lyases. Appl. Biochem. Biotechnol. 12, 135-176
5. Lohse, D.L. and Linhardt, R.J. (1992) Purification and characterization of heparin lyases from Flavobacterium heparinum. J. Biol. Chem. 267, 24347-24355
6. Bellamy, R.W. and Horikoshi, K. (1992) Heparinase produced by microorganism belonging to the genus Bacillus in US Patent, Research Development Corporation of Japan
7. Watanabe, M., Tsuda H., Yamada S., Shibata, Y., Nakamura T., and Sugahara, K. (1998) Characterization of heparinase from an oral bacterium Prevotella heparinolytica. J. Biochem. 123, 283-288
8. Kim, B.T., Kim, W.S, Kim, Y.S., Linhardt, R.J., and Kim, D.H. (2000) Purification and characterization of a novel heparinase from Bacteroides stercoris HJ-15. J. Biochem. 128, 323-328
9. Ernest, S., Venkataraman, G., Winkler, S., Godavarti R., Longer, R., and Coony, CL. (1996) Enzymatic degradation of glycosaminoglycans. Biochem. J. 315, 589-597
10. Godavarti, R., Davis, M., Venkartaraman, G., Coony, C.L., Longer, R., and Sasisekharan, R. (1996) A comparative analysis of the primary sequences and characteristics of heparinase I, II and III from Flavobacterium heparinum. Biochem. Biophys. Res. Commun. 225, 751-758
11. Godavarti, R., Coony, C.L., Langer, R., and Sasisekharan, R. (1996) Heparinase I from Flavobacterium heparinum. Identification of a critical histidine residue essential for catalysis as probed by chemical modification and site-directed mutagenesis. Biochemistry 35, 4846-6854
12. Sasisekharan, R., Bulmer, M., Morenan, K.W., Coony, C.L., and Longer, R. (1993) Cloning and expression of heparinase I gene from Flavobacterium heparinum. Proc. Natl Acad. Sci. USA 90, 3660-3664
13. Su, H., Blain, F., Musil, R.A., Zimmermann, J.J.F., Gu, K., and Bennet, D.C. (1996) Isolation and expression in Eschericha coli of hepB and hepC genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum. Appl. Environ. Microbiol. 62, 2723-2734
14. Ernest, S., Langer, R., Coony, C.L., and Sasisekharan, R. (1995) Enzymatic degradation of glycosaminoglycans. CRC Crit. Rev. Biochem. Mol. Biol. 30, 387-444
15. Sasisekharan, R., Leckbond, D., Godavarti, R., Venkataraman, G., Coony, C.L., and Longer R. (1995) Heparinase I from Flavobacterium heparinum: The role of cysteine residues in catalysis as probed by chemical modification and site-directed mutagenesis. Biochemistry 34, 14441-14448
16. Shriver, Z., Hu, Y., Pojasek, K., and Sasisekharan, R. (1998) Heparinase II from Flavobacterium heparinum-Role of cysteine in enzymatic activity as probed by chemical modification and site-directed mutagenesis. J. Biol. Chem. 273, 22904-22912
17. Bradford, M.M. (1976) A rapid and sensitive method for the quatitation of microgram quatities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
18. Zimmerman, Joseph, J.F., Oddie, K., Langer, R., and Coony, C.L. (1991) Release of heparinase by three step osmotic shock. Appl. Biochem. Biotechnol. 30, 137-148
19. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227, 680-685
20. Yang, V.C., Linhardt, R.J., Berstein, H., Coony C.L., and Langer, R. (1985) Purification and characterization of heparinase from Flavobacterium heparinum. J. Biol. Chem. 260, 1849-1857
21. Yang, V.C., Berstein, H., Coony C.L., and Langer, R. (1987) Large scale preparation and characterization of mucopolysaccharase contamination free heparinase. Appl. Biochem. Biotechnol. 16, 35-50
22. Moffat, C.F., Mclean, M.W., and Long, W.F. (1991) Heparinase II from Flavobacterium heparinum- Action of chemically modified heparins. Eur. J. Biochem. 197, 449-459