U.S. patents available from 1976 to present.
U.S. patent applications available from 2005 to present.

Methods for purifying and isolating recombinant chondroitinases

Patent 7129335 Issued on October 31, 2006. Estimated Expiration Date: Icon_subject October 14, 2024. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.

Patent References

Process for producing heparinase
Patent #: 4341869
Issued on: 07/27/1982
Inventor: Langer, Jr. ,   et al.

Heparinase produced by microorganism belonging to the genus bacillus
Patent #: 5145778
Issued on: 09/08/1992
Inventor: Bellamy, et al.

Large scale method for purification of high purity heparinase from flavobacterium heparinum
Patent #: 5169772
Issued on: 12/08/1992
Inventor: Zimmerman, et al.

Purification of glycosaminoglycan degrading enzymes with a sulfated polysaccharide
Patent #: 5198355
Issued on: 03/30/1993
Inventor: Kikuchi, et al.

Exposure compensation device of camera
Patent #: 5198855
Issued on: 03/30/1993
Inventor: Iwai

Heparitinase, process for producing the same and bacteria producing the same
Patent #: 5290695
Issued on: 03/01/1994
Inventor: Morikawa, et al.

Heparinase free of an anticoagulant component from flavobacterium Heparinum
Patent #: 5338677
Issued on: 08/16/1994
Inventor: Zimmermann, et al.

Purification of heparinase I, II, and III from Flavobacterium heparinum
Patent #: 5389539
Issued on: 02/14/1995
Inventor: Sasisekharan, et al.

Chondroitinase ABC isolated from proteus vulgaris ATCC 6896
Patent #: 5496718
Issued on: 03/05/1996
Inventor: Hashimoto, et al.

Chondroitinase II from Proteus vulgaris
Patent #: 5498536
Issued on: 03/12/1996
Inventor: Khandke

More ...

Inventors

Application

No. 10966671 filed on 10/14/2004

US Classes:

530/412, Separation or purification435/232, Lyase (4. )536/23.2, Encodes an enzyme435/200Acting on glycosyl compound (3.2)

Examiners

Primary: Saidha, Tekchand

Attorney, Agent or Firm

Foreign Patent References

  • 0355831 EP 02/01/1990
  • 0 613 949 EP 09/01/1994
  • 1 607 478 EP 12/01/2005
  • 54107586 JP 08/01/1979
  • 2000044601 JP 02/01/2000
  • WO 91/16070 WO 10/01/1991
  • WO 93/08289 WO 04/01/1993
  • WO 94/12618 WO 06/01/1994
  • WO 95/13830 WO 05/01/1995
  • WO 95/34635 WO 12/01/1995
  • WO 96/01648 WO 01/01/1996
  • WO 96/01894 WO 01/01/1996
  • WO 97/16556 WO 05/01/1997
  • WO 97/18835 WO 05/01/1997
  • WO 99/58650 WO 11/01/1999
  • WO 200139795 WO 02/01/2000
  • WO 01/34781 WO 05/01/2001
  • WO 01/35977 WO 05/01/2001
  • WO 01/38399 WO 05/01/2001
  • WO 01/53474 WO 07/01/2001
  • WO 03/074080 WO 09/01/2003
  • WO 2004/110360 WO 12/01/2004
  • WO 2005/112986 WO 12/01/2005

International Classes

A23J 1/00
C12N 9/88
C07H 21/04

Abstract

The invention relates to rationally designed polysaccharide lyases and uses thereof. In particular, the invention relates to modified chondroitinase B. The modified chondroitinase B enzymes of the invention are useful for a variety of purposes, including cleaving and sequencing polysaccharides such as glycosaminoglycans (GAGs) as well as removing polysaccharides from a solution. The invention also includes methods of inhibiting anticoagulant activity, inhibiting angiogenesis, treating cancer, and inhibiting maternal malarial infection.

Other References

  • Achur et al., “Characterization of Proteoglycans of Human Placenta and Identification of Unique Chondroitin Sulfate Proteoglycans of the Intervillous Spaces that Mediate the Adherence of Plasmodium falciparum-infected Erythrocytes to the Placenta,” The Journal of Biological Chemistry, vol. 275(51), Dec. 22, 2000, pp. 40344-40356.
  • Alkhalil et al., “Structural Requirements for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin Sulfate Proteoglycans of Human Placenta,” The Journal of Biological Chemistry, vol. 275(51), Dec. 22, 2000, pp. 40357-40364.
  • Baker, J. R. et al., “Action Pattern and Substrate Specificity of the Hyaluronan Lyase from Group B Streptococci”, Biochem. J., vol. 348, 2000, pp. 465-471.
  • Catlow et al., “Hepatocyte Growth Factor/scatter Factor and its Interaction With Heparan Sulphate and Dermatan Sulphate”, Biochemical Society Transactions, 2003, vol. 31(Part 2), pp. 352-353.
  • Daidouji et al., “Neoplastic Changes in Saccharide Sequence of Dermatan Sulfate Chains Derived from Human Colon Cancer,” Digestive Diseases and Sciences, vol. 47(2) Feb. 2002, pp. 331-337.
  • Denholm et al., “Anti-Tumor Activities of Chondroitinase AC and Chondroitinase B: Inhibition of Angiogenesis, Proliferation and Invasion,” European Journal of Pharmacology, vol. 416, 2001, pp. 213-221.
  • Denholm et al., “Inhibition of Human Dermal Fibroblast Proliferation by Removal of Dermatan Sulfate,” European Journal of Pharmacology, vol. 400, 2000, pp. 145-153.
  • Dierks et al., “Posttranslational Formation of Formylglycine in Prokaryotic Sulfatases by Modification of Either Cysteine or Serine”, The Journal of Biological Chemistry, vol. 273(40), Oct. 2, 1998, pp. 25560-25564.
  • Ernst, S. et al., “Enzymatic Degradation of Glycosaminoglycans” Critical Reviews in Biochemistry and Molecular Biology, vol. 30(5), 1995, pp. 387-444.
  • Ernst, S. et al., “Direct Evidence for a Predominantly Exolytic Processive Mechanism for Depolymerization of Heparin-like Glycosaminoglycans by Heparinase I”, Proceedings of the National Academy of Sciences of the United States of America, vol. 95, Apr. 1998, pp. 4182-4187.
  • Gacesa et al., “Enzymic Degradation of Alginates”, International Journal of Biochemistry, vol. 24(4), 1992, pp. 545-552.
  • Gandra et al., “Anticoagulant Sulfated Glycosaminoglycans in the Tissues of the Primitive Chordate Styela plicata (Tunicata)”, Glycobiology, vol. 10(12), 2000, pp. 1333-1340.
  • Gerit et al., “Understanding the Rates of Certain Enzyme-Catalyzed Reactions: Proton Abstraction from Carbon Acids, Acyl-Transfer Reactions and Displacement Reactions of Phosphodiesters”, Biochemistry, vol. 32(45), Nov. 16, 2003, pp. 11943-11952.
  • Gu, K. et al., “Purification, Characterization and Specificity of Chondroitin Lyases and Glycuronidase from Flavobacterium heparinum” Biochemistry Journal, vol. 312, 1995, pp. 569-577.
  • Habuchi, O., “Diversity and Functions of Glycosaminoglycan Sulfotransferases”, Biochimica Et Biophysica Acta, vol. 1474, 2000, pp. 115-127.
  • Homans, S. W., “A Molecular Mechanical Force Field for the Conformational Analysis of Oligosaccharides: Comparison of Theoretical and Crystal Structures of Manα1-3Manβ1-4GlcNAc”, Biochemistry, vol. 29, 1990, pp. 9110-9118.
  • Huang et al., “Crystal Structure of Chondroitinase B from Flavobacterium heparinum and Its Complex with a Disaccharide Product at 1.7 Å Resolution,” The Journal of Molecular Biology, vol. 294, 1999, pp. 1257-1269.
  • Huang, W. et al., “Active Site of Chondroitin AC Lyase Revealed by the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis”, Biochemistry, vol. 40, 2001, pp. 2359-2372.
  • Huige, C. J. M. et al., “Force Field Parameters for Sulfates and Sulfamates Based on Ab Initio Calculations: Extensions of AMBER and CHARMm Fields”, Journal of Computational Chemistry, vol. 16(1), 1995, pp. 56-79.
  • Jandik, K. A., et al., “Action Pattern of Polysaccharide Lyases on Glycosaminoglycans”, Glycobiology, vol. 4(3), 1994, pp. 289-296.
  • Jenkins et al., “The Architecture of Parallel β-Helices and Related Folds”, Progress in Biophysics & Molecular Biology, vol. 77, 2001, pp. 111-175.
  • Karamanos et al., “Identify of Dermatan and Chondroitin Sequences in Dermatan Sulfate Chains Determined by Using Fragmentation with Chondroitinases and Ion-Pair High-Performance Liquid Chromatography,” Analytical Biochemistry, vol. 225, 1995, pp. 220-230.
  • Lin, B. et al., “Identification of a Histidine Residue Essential for Enzymatic Activity of Group B Streptococcal Hyaluronate Lyase”, Biochemical and Biophysical Research Communications, vol. 231, 1997, pp. 379-382.
  • Liu, D. et al., “Tumor Cell Surface Heparan Sulfates as Cryptic Promoters or Inhibitors or Tumor Growth and Metastasis”, Proceedings of the National Academy of Sciences of the United States of America, vol. 99(2), Jan. 22, 2002, pp. 568-573.
  • Lyon et al., “Hepatocyte Growth Factor/Scatter Factor Binds with High Affinity to Dermatan Sulfate,” The Journal of Biological Chemistry, vol. 273(1), Jan. 2, 1998, pp. 271-278.
  • Lyon et al., “The Mode of Action of Heparan and Dermatan Sulfates in the Regulation of Hepatocyte Growth Factor/Scatter Factor,” The Journal of Biological Chemistry, vol. 277(2), Jan. 11, 2002, pp. 1040-1046.
  • Maimone, M. M. et al., “Structure of a Dermatan Sulfate Hexasaccharide that Binds to Heparin Cofactor II with High Affinity”, The Journal of Biological Chemistry, vol. 265, 1990, p. 14830.
  • Mascellani, G. et al., “Structure and Contribution to the Heparin Cofactor II-mediated Inhibition of Thrombin of Naturally Oversulphated Sequences of Dermatan Sulphate”, Biochemical Journal, vol. 296, 1993, pp. 639-648.
  • Michel et al., “The Structure of Chondroitin B Lyase Complexed with Glycosaminoglycan Oligosaccharides Unravels a Calcium-dependent Catalytic Machinery”, The Journal of Biological Chemistry, vol. 279(31), Jul. 30, 2004, pp. 32882-32896.
  • Mitropoulou et al., “Identification of Oligomeric Domains within Dermatan Sulfate Chains Using Differential Enzymic Treatments, Derivatization with 2-Aminoacridone and Capillary Electrophoresis,” Electrophoresis, vol. 22, 2001, pp. 2458-2463.
  • Monagle et al., “Covalent Heparin Cofactor II-Heparin and Heparin Cofactor II-Dermatan Sulfate Complexes,” The Journal of Biological Chemistry, vol. 273(50), Dec. 11, 1998, pp. 33566-33571.
  • Nadanaka, S. et al., “The Unusual Tetrasaccharide Sequence GlcAβ1-3GalNAc(4-sulfate)β1-4GlcA(2-sulfate)β1-3GalNAc(6-sulfate) found in the Hexasaccharides Prepared by Testicular Hyaluronidase Digestion of Shark Cartilage Chondroitin Sulfate D” Glycobiology, vol. 7(2), 1997, pp. 253-263.
  • Pagès, S. et al., Changing a Single Amino Acid Residue Switches Processive and Non-processive Behavior of Aspergillus niger Endopolygalacturonase I and II, The Journal of Biological Chemistry, vol. 276(36), Sep. 7, 2001, pp. 33652-33656.
  • Pervin et al., “Capillary Electrophoresis to Measure Sulfoesterase Activity on Chondroitin Sulfate and Heparin Derived Disaccharides”, Applied and Theoretical Electrophoresis, vol. 3, 2003, pp. 297-303.
  • Plaas et al., “Glycosaminoglycan Sulfation in Human Osteoarthritis,” The Journal of Biological Chemistry, vol. 273(20), May 15, 1998, pp. 12642-12649.
  • Pojasek et al., Recombinant Expression, Purification, and Kinetic Characterization of Chondroitinase AC and Chondroitinase B from Flavobacterium heparinum, Biochemical and Biophysical Research Communications, vol. 286, 2001, pp. 343-351.
  • Pojasek K. et al., “Biochemical Characterization of the Chondroitinase B Active Site”, The Journal of Biological Chemistry, vol. 277(34), Aug. 23, 2002, pp. 31179-31186.
  • Pojasek et al., Histidine 295 and Histidine 510 Are Crucial for the Enzymatic Degradation of Heparan Sulfate by Heparinase III, Biochemistry, vol. 39, 2000. pp. 4012-4019.
  • Rhomberg, A. J. et al., “Mass Spectrometric and Capillary Electrophoretic Investigation of the Enzymatic Degradation of Heparin-like Glycosaminoglycans”, Proceedings of the National Academy of Sciences of the United States of America, vol. 95, Apr. 1998, pp. 4176-4181.
  • Rhomberg, A. J. et al., “Mass Spectrometric Evidence for the Enzymatic Mechanisms of the Depolymerization of Heparin-like Glycosaminoglycans by Heparinase II”, Proceedings of the National Academy of Sciences of the United States of America, vol. 95, Oct. 1998, pp. 12232-12237.
  • Roy, C. et al., “Modes of Action of Five Different Endopectate Lyases from Erwinia chrysantehmi 3937” Journal of Bacteriology, vol. 181(12), Jun. 1999, pp. 3705-3709.
  • Sasisekharan, R. et al., “Cloning and Expression of Heparinase I Gene from Flavobacterium heparinum” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, Apr. 1993, pp. 3660-3664.
  • Sasisekharan, R. et al., “Heparinase I from Flavobacterium heparinum” The Journal of Biological Chemistry, vol. 271(6), Feb. 9, 1996, pp. 3124-3131.
  • Scavetta, R. D. et al., “Structure of a Plant Cell Wall Fragment Complexed to Pectate Lyase C”, The Plant Cell, vol. 11, Jun. 1999, pp. 1081-1092.
  • Shriver et al., “Sequencing of 3-O Sulfate Containing heparin Decasaccharides with a Partial Antithrombin III Binding Site”, Proceedings of the National Academy of Sciences of the United States of America, vol. 97(19), Sep. 12, 2000, pp. 10359-10364.
  • Shriver et al., “Cleavage of the Antithrombin III Binding Site in Heparin by Heparinases and its Implication in the Generation of Low Molecular Weight Heparin”, Proceedings of the National Academy of Sciences of the United States of America, vol. 97(19), Sep. 12, 2000, pp. 10365-10370.
  • Shriver, Z. et al., “Heparinase II from Flavobacterium heparinum: . . . ”, The Journal of Biological Chemistry, vol. 273(17), Apr. 24, 1998, pp. 10160-10167.
  • Shriver, Z. et al., “Heparinase II from Flavobacterium heparium: . . . ”, The Journal of Biological Chemistry, vol. 273(36), Sep. 4, 1998, pp. 22904-22912.
  • Shriver, Z. et al., “Emerging Views of Heparan Sulfate Glycosaminoglycan Structure/Activity Relationships Modulating Dynamic Biological Functions” Trends Cardiovascular Med., vol. 12(2), 2002, pp. 71-77.
  • Steinbacher, S. et al.,“Crystal Structure of P22 Tailspike Protein: Interdigitated Subunits in a Thermostable Trimer”, Science, vol. 265(5170), Jul. 15, 1994, pp. 383-386.
  • Sugahara, K. et al., “Novel Sulfated Oligosaccharides Containing 3-O-Sulfated Glucuronic Acid from King Crab Cartilage Chondroitin Sulfate K . . . ”, The Journal of Biological Chemistry, vol. 271(43), Oct. 25, 1996, pp. 26745-26754.
  • Sundaram et al., “Rational Design of Low-Molecular Weight Heparins with Improved In Vivo Activity”, Proceedings of the National Academy of Sciences of the United States of America, vol. 100(2), Jan. 21, 2003, pp. 651-656.
  • Trowbridge et al., “Dermatan Sulfate Binds and Potentiates Activity of Keratinocyte Growth Factor (FGF-7),” The Journal of Biological Chemistry, vol. 277(45), Nov. 8, 2002, pp. 42815-42820.
  • Trowbridge et al., “Dermatan Sulfate: New Functions from an Old Glycosaminoglycan,” Glycobiology, vol. 12(9), 2002, pp. 117R-125R.
  • Tumova, S. et al., “Heparan Sulfate Proteoglycans on the Cell Surface: Versatile Coordinators of Cellular Functions”, The International Journal of Biochemistry & Cell Biology, vol. 32, 2000, pp. 269-288.
  • Ueoka, C. et al., “Structural Determination of Novel Tetra- and Hexasaccharide Sequences Isolated from Chondroitin Sulfate H (Oversulfated Dermatan Sulfate) of Hagfish Notochord”, Glycoconjugate Journal, vol. 16, 1999, pp. 291-305.
  • van den Hoogen, B. M. et al., “A Microtiter Plate Assay for the Determination of Uronic Acids”, Analytical Biochemistry, vol. 257, 1998, pp. 107-111.
  • Venkataraman, G. et al., “A Stereochemical Approach to Pyranose Ring Flexibility: Its Implications for the Conformation of Dermatan Sulfate”, Proceedings of the National Academy of Sciences of the United States of America, vol. 91, Jun. 1994, pp. 6171-6175.
  • Venkataraman, G. et al., “Sequencing Complex Polysaccharides”, Science, vol. 286, Oct. 15, 1999, pp. 537-542.
  • Vicente, C.P. et al., “Unbalanced Effects of Dermatan Sulfates with Different Sulfation Patterns on Coagulation, Thrombosis and Bleeding”, Thromb. Haemost., vol. 86, 2001, pp. 1215-1220.
  • Yang, H.O. et al., “Preparation and Structural Determination of a Dermatan Sulfate-Derived Oligosaccharides”, Glycobiology, vol. 10(10), 2000, pp. 1033-1039.
  • Yoder et al., “The Refined Three-Dimensional Structure of Pectate Lyase C . . . ,” Plant Physiol., vol. 107, 1995, pp. 349-364.
  • NCBI database, Protein IDBGA Chain A. Crystal Structure of Chondroitinase B, Accession No. 6980641.
  • NCBI database, Protein IDBOA Chain A. Crystal Structure of Chondroitinase B, Accession No. 6980642.
  • NCBI database, “Pedobacter Heparinus Chondroitinase B Precursor (cs1B) gene Complete cds”, Accession No. U27584.1 GI:1002526.
  • NCBI database, Structure Summary IDBO, Crystal Structure of Chondroitinase B, MMDB No. 12452.
  • Protein Data Bank, Structure Explorer—1DBO, “Crystal Structure of Chondroitinase B” http://www.rcsb.org/pdb/cgi/explore.cgi/ex:ore.cgi?pdbld=1DBO, printed Feb. 23, 2005, 1 page.
  • Structure Summary Printout for 1dbo, http://pdbbeta.rcsb.org/pdb/explore.do?structureld=ldbo, printed Feb. 23, 2005, 1 page.
  • NCBI database, Structure Summary for 1DBG, Crystal Structure of Chondroitinase B, MMDB No. 12451.
  • Structure Summary Printout for Idbg, http://pdbbeta.rcsb.org/pdb/explore.do?structureId=ldbg, printed Feb. 23, 2005, 1 page.
  • Protein Data Bank, Structure Explorer—1DBG, “Crystal Structure of Chondroitinase B”, http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=lDBG, printed Feb. 23, 2005, 1 page.
  • NCBI Database, Structure Summary for 1HM2, Crystal Structure of Chondroitinase B, MMDB No. 16157.
  • Protein Data Bank, Structure Explorer—1HM2, “Active Site of Chondroitinase Ac Lyase Revealed by The Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis”, http://www/rcsb.org/pdb/cgi/explore.cgi?pdbId=1HM2, printed Feb. 23, 2005, 1 page.
  • Structure Summary Printout for lHM2, http://pdbbeta.rcsb.org/pdb/explore.do?structureId=1hm2, printed Feb. 23, 2005, 2 pages.
  • NCBI Database, Structure Summary for 1PLU, “Pectate Lyase from Erwinia Chrysanthemi . . . ”, MMDB No. 10896.
  • Protein Data Bank, Structure Explorer—1PLU, “Pectate Lyase C From Erwinia Chrysanthemi With 1 Lu+3 Ion in the Putative Calcium Binding Site”, http://rcsb.org/pdb/cgi/explore.cgi?pdbId=1PLU, printed Feb. 23, 2005, p. 1.
  • Structure Summary Printout for 1plu, “Pectate Lyase C From Erwinia Chrysanthemi With 1 Lu+3 Ion in the Putative Calcium Binding Site”, http://pdbbeta.rcsb.org/pdb/explore.do?structureId=1plu, printed Feb. 23, 2005, 1 page.
  • Tkalec, A.L. et al., “Isolation and Expression in Escherichia coli of cslA and cslB, Genes Coding for the Chondroitin Sulfate-Degrading Enzymes Chondroitinase AC and Chondroitinase B, Respectively from Flavobacterium heparium”, Applied and Environmental Microbiology, 2000, pp. 29-35.
  • Theocharis D.A., et al., “Determination and structural Characterisation of Dermatan Sulfate in the Presence of Other Galactosaminoglycans”, Journal of Chromatography B, vol. 754(2), Apr. 25, 2001, pp. 297-309.—Abstract Only.
  • Yunge et al., “Crystallization and Preliminary X-ray Analysis of Chondroitinase B from Flavobacterium heparium”, Acta Crystallographica Section D Biological Crystallography, vol. 55(5), May 1999, pp. 1055-1057.—Abstract Only.
  • Aguiar et al., Preparation and purification of Flavobacterium heparium chondroitinase AC and B by hydrophobic interaction chromatography. Braz J Med Biol Res. May 1999;32(5):545-50. Abstract Only.
  • Bernstein et al., Immobilized heparin lyase system for blood deheparinization. Methods in Enzymol. 1988;46:515-29.
  • Conrad et al., Structure of heparan sulfate and dermatan sulfate. Ann N Y Acad Sci. 1989;556:18-28.
  • Desai et al., Specificity studies on the heparin lyases from Flavobacterium heparium. Biochemistry. Aug. 17, 1993;32(32):8140-5.
  • Dietrich et al., Enzymatic degradation of heparin. A glucosaminidase and a glycuronidase from Flavobacterium heparium. Biochemistry. May 1969;8(5):2089-94.
  • Dietrich et al., Sequential degradation of heparin in Flavobacterium heparium. Purification and properties of five enzymes involved in heparin degradation. J Biol Chem. Sep. 25, 1973;248(18):6408-15.
  • Ernst et al., Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum. Biochem J. Apr. 15, 1996;315 ( Pt 2):589-97.
  • Gacesa et al., Alginate-modifying enzymes: A proposed unified mechanism of action for the lyases and epimerase. FEBS. Feb. 1987;212(2):199-202.
  • Gioldassi et al., Determination of phosphorylated and sulfated linkage-region oligosaccharides in chondroitin / dematan and heparan sulfate proteoglycans by high performance liquid chromatography. J Liq Chrom Rel Technol. 1999;22(13):1997-2007.
  • Godavarti et al., Heparinase I from Flavobacterium heparium. Identification of a critical histidine residue essential for catalysis as probed by chemical modification and site-directed mutagenesis. Biochemistry. May 28, 1996;35(21):6846-52.
  • Godavarti et al., Heparinase I from Flavobacterium heparium. Role of positive charge in enzymatic activity. J Biol Chem. Jan. 2, 1998;273(1):248-55.
  • Godavarti et al., Heparinase III from Flavobacterium heparium: cloning and recombinant expression in Escherichia coli. Biochem Biophys Res Commun. Aug. 23, 1996;225(3):751-8.
  • Godavarti et al., A comparative analysis of the primary sequences and characteristics of heparinases I, II, and III from Flavobacterium heparinum. Biochem Biophys Res Commun. Dec. 24, 1996;229(3):770-7.
  • Hashimoto et al., Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch Biochem Biophys. Aug. 15, 1999;368(2)367-74.
  • Hovingh et al., Specificity of flavobacterial glycuronidases acting on disaccharides derived from glycosaminoglycans. Biochem J. Aug. 1, 1977;165(2):287-93.
  • Hulett et al., Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis. Nat Med. Jul. 1999;5(7):803-9.
  • Kjellen et al., Proteoglycans: structures and interactions. Annu Rev Biochem. 1991;60:443-75.
  • Liu et al., Strategy for the sequence analysis of heparin. Glycobiology. Dec. 1995;5(8):765-74.
  • Liu et al., The calcium-binding sites of heparinase I from Flavobacterium heparium are essential for enzymatic activity. J Biol Chem. Feb. 12, 1999;274(7):4089-95.
  • Liu et al., Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues. J Biol Chem. Dec. 31, 1999;274(53):38155-62.
  • Lohse et al., Purification and characterization of heparin lyases from Flavobacterium heparinum. J Biol Chem. Dec. 5, 1992;267(34):24347-55.
  • McLean et al., Flavobacterium heparium 2-O-sulphatase for 2-O-sulphato-delta 4,5-glycuronate-terminated oligosaccharides from heparin. Eur. J Biochem, Dec. 17, 1984;145(3):607-15.
  • Murata et al., Characterization of the products generated from oversulphated dermatan sulphate isomers with chondroitinase-B by high-performance liquid chromatography. J Chromatogr. Dec. 25, 1987;423:51-61. Abstract Only.
  • Myette et al., Molecular cloning of the heparin/heparan sulfate delta 4,5 unsaturated glycuronidase from Flavobacterium heparinum, its recombinant expression in Escherichia coli, and biochemical determination of its unique substrate specificity. Biochemistry. Jun. 11, 2002;41(23):7424-34.
  • Myette et al., Expression in Escherichia coli, purification and kinetic characterization of human heparan sulfate 3-O-sulfotransferase-1, Biochem Biophys Res Commun. Feb. 1, 2002;290(4):1206-13.
  • Myette et al., The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparinum. Molecular cloning, recombinant expression, and biochemical characterization. J Biol Chem. Apr. 4, 2003;278(14):12157-66.
  • Nakano et al., Study of sulfated glycosaminoglycans from porcine skeletal muscle epimysium including analysis of iduronosyl and glucuronosyl residues in galactosaminoglycan fractions. J. Agricult and Food Chem. 1996;44(6):1424-34. Abstract Only.
  • Petitou et al., Synthetic oligosaccharides having various functional domains: potent and potentially safe heparin mimetics. Bioorg Med Chem Lett. Apr. 19, 1999;9(8):1161-6.
  • Prabhakar et al., Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant expression and active site identification. Biochem J. Feb. 15, 2005;386(Pt 1):103-12.
  • Prabhakar et al., Biochemical characterization of the chondroitinase ABC I active site. Biochem J. Sep. 1, 2005;390(Pt 2):395-405.
  • Raman et al., Structural insights into biological roles of protein-glycosaminoglycan interactions. Chem Biol. Mar. 2005;12(3):267-77.
  • Raman et al., The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparium. A structural and biochemical study of the enzyme active site and saccharide substrate specificity. J Biol Chem. Apr. 4, 2003;278(14):12167-74.
  • Razi et al., Structural and functional properties of heparin analogues obtained by chemical sulphation of Escherichia coli K5 capsular polysaccharide. Biochem J. Jul. 15, 1995;309 (Pt 2):465-72.
  • Sasisekharan et al., Heparinase I from Flavobacterium heparinum: the role of the cysteine residue in catalysis as probed by chemical modification and site-directed mutagenesis. Biochemistry. Nov. 7, 1995;34(44):14441-8.
  • Sasisekharan et al., Heparinase inhibits neovascularization. Proc Natl Acad Sci U S A. Feb. 15, 1994;91(4):1524-8.
  • Satake et al., Enzymatic determination of urinary glycosaminoglycans from orthopedic patients. Tohoku J Exp Med. May 1983;140(1):89-96. Abstract Only.
  • Sato et al., Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase. Appl Microbiol Biotechnol. Mar. 1994;41(1):39-46.
  • Shriver et al., Biochemical investigations and mapping of the calcium-binding sites of heparinase I from Flavobacterium heparinum. J Biol Chem. Feb. 12, 1999;274(7):4082-8.
  • Takagaki et al., Analysis of glycosaminoglycans by high-performance liquid chromatography. J Biochem Biophys Methods. Jun. 1994;28(4):313-20. Abstract Only.
  • Vlodavsky et al., Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis. Nat Med. Jul. 1999;5(7):793-802.
  • Xiang et al., A method to increase contaminant tolerance in protein matrix-assisted laser desorption/ionization by the fabrication of thin protein-doped polycrystalline films. Rapid Comm in Mass Spect. 1994;8:199-204.
  • Warnick et al., Purification of an unusual -glycuronidase from flavobacteria. Biochemistry. Feb. 15, 1972;11(4):568-72.
  • Yang et al., Purification and characterization of heparinase from Flavobacterium heparinum. J Biol Chem. 1985;260(3):1849-57.
  • Yates et al., 1H and 13C NMR spectral assignments of the major sequences of twelve systemically modified heparin derivatives. Carbohydr Res. Nov. 20, 1996;294:15-27.
  • Yoder et al., New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science. Jun. 4, 1993;260(5113):1503-7.
  • Yoder et al., Unusual structural features in the parallel beta-helix in pectate lyases. Structure. Dec. 15, 1993;1(4):241-51.
  • Yosizawa et al., A simple method for the quantitation of glycuronic acid-containing glycosaminoglycans with mucopolysaccharidases. Anal Biochem. Jan. 1983;128(1):250-6. Abstract.
  • Zhang et al., 6-O-sulfotransferase-1 represents a critical enzyme in the anticoagulant heparan sulfate biosynthetic pathway. J Biol Chem. Nov. 9, 2001;276(45):42311-21.
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