References
- Ahn, M. Y., Shin, K. H., Kim, D. H., Jung, E. A., Toida, T., Linhardt, R. J. and Kim, Y. S. (1998) Characterization of a Bacteroides sp. from human intestine that degrades glycosaminoglycans. Can. J. Microbiol. 44, 423-429. https://doi.org/10.1139/cjm-44-5-423
- Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254. https://doi.org/10.1016/0003-2697(76)90527-3
- Castellot, J. J., Jr., Choay, J., Lormeau, J. C., Petitou, M., Sache, E. and Karnovsky, M. J. (1986) Structural determinants of the capacity of heparin to inhibit the proliferation of vascular smooth muscle cells. II. Evidence for a pentasaccharide sequence that contains a 3-O-sulfate group. J. Cell. Biol. 102, 1979-1984. https://doi.org/10.1083/jcb.102.5.1979
- Conrad, H. E. (1989) Structure of heparan sulfate and dermatan sulfate. Ann. N. Y. Acad. Sci. 556, 18-28. https://doi.org/10.1111/j.1749-6632.1989.tb22486.x
- Ernst, S., Venkataraman, G., Winkler, S., Godavarti, R., Langer, R., Cooney, C. L. and Sasisekharan, R. (1996) Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum. Biochem. J. 315, 589-597.
- Godavarti, R., Cooney, C. L., Langer, R. and Sasisekharan, R. (1996a) 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, 6846-6852. https://doi.org/10.1021/bi960356g
- Godavarti, R., Davis, M., Venkataraman, G., Cooney, C., Langer, R. and Sasisekharan, R. (1996b) Heparinase III from Flavobacterium heparinum: cloning and recombinant expression in Escherichia coli. Biochem. Biophys. Res. Commun. 225, 751-758. https://doi.org/10.1006/bbrc.1996.1246
- Godavarti, R. and Sasisekharan, R. (1998) Heparinase I from Flavobacterium heparinum. Role of positive charge in enzymatic activity. J. Biol. Chem. 273, 248-255. https://doi.org/10.1074/jbc.273.1.248
- Griffin, C. C., Linhardt, R. J., Van Gorp, C. L., Toida, T., Hileman, R. E., Schubert, R. L., 2nd and Brown, S. E. (1995) Isolation and characterization of heparan sulfate from crude porcine intestinal mucosal peptidoglycan heparin. Carbohydr. Res. 276, 183-197.
- Heres, E. K., Horrow, J. C., Gravlee, G. P., Tardiff, B. E., Luber, J., Jr., Schneider, J., Barragry, T. and Broughton, R. (2001) A dose-determining trial of heparinase-I (Neutralase) for heparin neutralization in coronary artery surgery. Anesth. Analg. 93, 1446-1452. https://doi.org/10.1097/00000539-200112000-00019
- Ishihara, M., Kariya, Y., Kikuchi, H., Minamisawa, T. and Yoshida, K. (1997) Importance of 2-O-sulfate groups of uronate residues in heparin for activation of FGF-1 and FGF-2. J. Biochem. Tokyo 121, 345-349. https://doi.org/10.1093/oxfordjournals.jbchem.a021593
- Jackson, R. L., Busch, S. J. and Cardin, A. D. (1991) Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 71, 481-539.
- Kim, B. T., Hong, S. W., Kim, W. S., Kim, Y. S. and Kim, D. H. (2001) Purification and characterization of acharan sulfate lyases, two novel heparinases, from Bacteroides stercoris HJ- 15. Eur. J. Biochem. 268, 2635-2641. https://doi.org/10.1046/j.1432-1327.2001.02156.x
- 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. Tokyo. 128, 323-328. https://doi.org/10.1093/oxfordjournals.jbchem.a022756
- Kim, Y. S., Jo, Y. Y., Chang, I. M., Toida, T., Park, Y. and Linhardt, R. J. (1996) A new glycosaminoglycan from the giant African snail Achatina fulica. J. Biol. Chem. 271, 11750-11755. https://doi.org/10.1074/jbc.271.20.11750
- Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
- Lindahl, U., Lidholt, K., Spillmann, D. and Kjellen, L. (1994) More to 'heparin' than anticoagulation. Thromb. Res. 75, 1-32. https://doi.org/10.1016/0049-3848(94)90136-8
- Linhardt, R. J., Turnbull, J. E., Wang, H. M., Loganathan, D. and Gallagher, J. T. (1990) Examination of the substrate specificity of heparin and heparan sulfate lyases. Biochemistry 29, 2611-2617. https://doi.org/10.1021/bi00462a026
- Lohse, D. L. and Linhardt, R. J. (1992) Purification and characterization of heparin lyases from Flavobacterium heparinum. J. Biol. Chem. 267, 24347-24355.
- Sasisekharan, R., Bulmer, M., Moremen, K. W., Cooney, C. L. and Langer, R. (1993) Cloning and expression of heparinase I gene from Flavobacterium heparinum. Proc. Natl. Acad. Sci. USA 90, 3660-3664. https://doi.org/10.1073/pnas.90.8.3660
- Sasisekharan, R., Moses, M. A., Nugent, M. A., Cooney, C. L. and Langer, R. (1994) Heparinase inhibits neovascularization. Proc. Natl. Acad. Sci. USA 91, 1524-1528. https://doi.org/10.1073/pnas.91.4.1524
- 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. Tokyo 123, 283-288. https://doi.org/10.1093/oxfordjournals.jbchem.a021934
- Yang, V. C., Linhardt, R. J., Bernstein, H., Cooney, C. L. and Langer, R. (1985) Purification and characterization of heparinase from Flavobacterium heparinum. J. Biol. Chem. 260, 1849-1857.
- Yoshida, E., Arakawa, S., Matsunaga, T., Toriumi, S., Tokuyama, S., Morikawa, K. and Tahara, Y. (2002) Cloning, sequencing, and expression of the gene from Bacillus circulans that codes for a heparinase that degrades both heparin and heparan sulfate. Biosci. Biotechnol. Biochem. 66, 1873-1879. https://doi.org/10.1271/bbb.66.1873
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