CA2493509A1 - Rationally designed polysaccharide lyases derived from chondroitinase b - Google Patents

Rationally designed polysaccharide lyases derived from chondroitinase b Download PDF

Info

Publication number
CA2493509A1
CA2493509A1 CA002493509A CA2493509A CA2493509A1 CA 2493509 A1 CA2493509 A1 CA 2493509A1 CA 002493509 A CA002493509 A CA 002493509A CA 2493509 A CA2493509 A CA 2493509A CA 2493509 A1 CA2493509 A1 CA 2493509A1
Authority
CA
Canada
Prior art keywords
chondroitinase
modified
recombinant
amino acid
native
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
CA002493509A
Other languages
French (fr)
Other versions
CA2493509C (en
Inventor
Kevin Pojasek
Rahul Raman
Ram Sasisekharan
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Massachusetts Institute of Technology
Original Assignee
Individual
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Individual filed Critical Individual
Publication of CA2493509A1 publication Critical patent/CA2493509A1/en
Application granted granted Critical
Publication of CA2493509C publication Critical patent/CA2493509C/en
Anticipated expiration legal-status Critical
Expired - Fee Related legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
    • C08B37/00—Preparation of polysaccharides not provided for in groups C08B1/00 - C08B35/00; Derivatives thereof
    • C08B37/006—Heteroglycans, i.e. polysaccharides having more than one sugar residue in the main chain in either alternating or less regular sequence; Gellans; Succinoglycans; Arabinogalactans; Tragacanth or gum tragacanth or traganth from Astragalus; Gum Karaya from Sterculia urens; Gum Ghatti from Anogeissus latifolia; Derivatives thereof
    • C08B37/0063—Glycosaminoglycans or mucopolysaccharides, e.g. keratan sulfate; Derivatives thereof, e.g. fucoidan
    • C08B37/0069—Chondroitin-4-sulfate, i.e. chondroitin sulfate A; Dermatan sulfate, i.e. chondroitin sulfate B or beta-heparin; Chondroitin-6-sulfate, i.e. chondroitin sulfate C; Derivatives thereof
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/88—Lyases (4.)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/527—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving lyase
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

Landscapes

  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • General Health & Medical Sciences (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Microbiology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Medicinal Chemistry (AREA)
  • Biophysics (AREA)
  • Dermatology (AREA)
  • Materials Engineering (AREA)
  • Biomedical Technology (AREA)
  • Physics & Mathematics (AREA)
  • Analytical Chemistry (AREA)
  • Polymers & Plastics (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Immunology (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Confectionery (AREA)
  • Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
  • Polysaccharides And Polysaccharide Derivatives (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
  • Immobilizing And Processing Of Enzymes And Microorganisms (AREA)

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 solutio n. The invention also includes methods of inhibiting anticoagulant activity, inhibiting angiogenesis, treating cancer, and inhibiting maternal malarial infection.

Claims (35)

1. A modified chondroitinase B having an amino acid sequence of the mature peptide of SEQ ID NO: 2 or conservative substitutions thereof, wherein at least one residue at a position selected from the group consisting of 116, 184, 213, 219, 245, 250, 271, 272, 296, 298, 318, 333, 363 and 364 of SEQ ID NO: 2 has been substituted or deleted.
2. The chondroitinase B of claim 1, wherein the substituted amino acid is a conservative amino acid substitution.
3. The chondroitinase B of claim 1, wherein the chondroitinase B is a substantially purified recombinant form.
4. A modified chondroitinase B having a modified product profile, wherein the modified product profile of the modified chondroitinase B is at least 10%
different than a native product profile of a native chondroitinase B.
5. The chondroitinase B of claim 4, wherein the modified chondroitinase B has a modified product profile that is at least 50% different than a native product profile of a native chondroitinase B.
6. The chondroitinase B of claim 4, wherein the modified chondroitinase B has a modified product profile that is at least 20% different than a native product profile of a native chondroitinase B.
7. The chondroitinase B of claim 4, wherein the modified chondroitinase B has the amino acid sequence of the mature peptide of SEQ ID NO: 2 wherein at least one amino acid residue has been substituted and wherein the substituted amino acid is at a position selected from the group consisting of 272, 333, and 364 of SEQ ID NO:
2.
8. A modified chondroitinase B having a k cat, or K M value for a substrate that is at least 10% different than a native chondroitinase B k cat or K M value.
9. The chondroitinase B of claim 8, wherein the modified chondroitinase B kcat or KM value is at least 20% different than a native chondroitinase B kcat or KM value.
10. The chondroitinase B of claim 8, wherein the modified chondroitinase B
kcat or KM value is at least 50% different than a native chondroitinase B kcat or KM value.
11. The chondroitinase B of claim 8, wherein the modified chondroitinase B has the amino acid sequence of the mature peptide of SEQ ID NO: 2 wherein at least one amino acid residue has been substituted and wherein the substituted amino acid is at a position selected from the group consisting of 272, 333, 363 and 364 of SEQ ID
NO: 2.
12. The chondroitinase B of claim 9, wherein the substrate is a glycosaminoglycan.
13. A pharmaceutical preparation comprising a sterile formulation of chondroitinase B of any one of claims 1-12 and a pharmaceutically acceptable carrier.
14. A method of specifically cleaving chondroitin sulfate, comprising:
contacting chondroitin sulfate with the chondroitinase B of any one of claims 12.
15. A method of specifically cleaving dermatan sulfate, comprising:
contacting dermatan sulfate with the chondroitinase B of any one of claims 1-12.
16. The method of claim 14, wherein the method is a method of removing chondroitin sulfate from a chondroitin sulfate containing fluid.
17. The method of claims 15, wherein the method is a method of removing dermatan sulfate from a dermatan sulfate containing fluid.
18. The method of claim 14, wherein the method is a method for sequencing chondroitin sulfate oligosaccharides.
19. The method of claim 15, wherein the method is a method for sequencing dermatan sulfate oligosaccharides.
20. A method of analyzing a sample of polysaccharides, comprising:
contacting the sample with the chondroitinase B of any one of claims 1-12.
21. A method of identifying the presence of a particular polysaccharide in a sample, comprising:
contacting the sample with the chondroitinase B of any one of claims 1-12.
22. A method of determining the purity of sample of polysaccharides, comprising:
contacting the sample with the chondroitinase B of any one of claims 1-12.
23. A method for determining the composition of a sample of polysaccharides, comprising:
contacting the sample with the chondroitinase B of any one of claims 1-12.
24. A method for inhibiting angiogenesis, comprising administering to a subject an effective amount for inhibiting angiogenesis of the chondroitinase B of any one of claims 1-12, or a GAG fragment produced by the chondroitinase B of any one of claims 1-12.
25. The method of claim 24 wherein the chondroitinase B or GAG fragment is administered to a tumor.
26. The method of claim 24, wherein the chondroitinase B or GAG fragment is administered in a biodegradable, biocompatible polymeric delivery device.
27. The method of claim 24, wherein the chondroitinase B or GAG fragment is administered in a pharmaceutically acceptable vehicle for injection.
28. An immobilized modified chondroitinase B comprising:
a modified chondroitinase B as in any one of claims 1-12, and a solid support membrane, wherein the modified chondroitinase B is immobilized on the solid support membrane.
29. A method for purifying a recombinant chondroitinase, comprising:
inducing a culture of cells containing a recombinant chondroitinase with an inducing agent for greater than four hours, and isolating the recombinant chondroitinase from the cells to produce a purified chondroitinase.
30. The method of claim 29, wherein the cells are incubated with the inducing agent at a temperature of between 20° and 26° C.
31. The method of claim 30, wherein the cells are incubated with the inducing agent for at least 8 hours.
32. The method of claims 29, wherein the chondroitinase is selected from the group consisting of chondroitinase AC and B.
33. The method of claim 29, wherein the recombinant chondroitinase includes an terminal Histidine tag.
34. The method of claim 33, further comprising passing the recombinant chondroitinase over a charged Ni 2+ column to isolate the recombinant chondroitinase.
35. A method for isolating a recombinant chondroitinase, comprising:
lysing a cell culture containing a recombinant chondroitinase having a terminal Histidine tag, and passing the recombinant chondroitinase over a charged Ni 2+ column to isolate the recombinant chondroitinase.
CA002493509A 2002-06-03 2003-06-03 Rationally designed polysaccharide lyases derived from chondroitinase b Expired - Fee Related CA2493509C (en)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
US38550902P 2002-06-03 2002-06-03
US60/385,509 2002-06-03
PCT/US2003/017680 WO2003102160A2 (en) 2002-06-03 2003-06-03 Rationally designed polysaccharide lyases derived from chondroitinase b

Publications (2)

Publication Number Publication Date
CA2493509A1 true CA2493509A1 (en) 2003-12-11
CA2493509C CA2493509C (en) 2010-03-09

Family

ID=29712183

Family Applications (1)

Application Number Title Priority Date Filing Date
CA002493509A Expired - Fee Related CA2493509C (en) 2002-06-03 2003-06-03 Rationally designed polysaccharide lyases derived from chondroitinase b

Country Status (7)

Country Link
US (4) US6962699B2 (en)
EP (1) EP1532241B1 (en)
AT (1) ATE481478T1 (en)
AU (1) AU2003243396A1 (en)
CA (1) CA2493509C (en)
DE (1) DE60334220D1 (en)
WO (1) WO2003102160A2 (en)

Families Citing this family (34)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2003527822A (en) 1998-08-27 2003-09-24 マサチューセッツ インスティテュート オブ テクノロジー Rationally designed heparinases from heparinases I and II
JP2002531217A (en) * 1998-12-04 2002-09-24 チャンドラシェカー ピー． パサック， Biocompatible crosslinked polymer
US7412332B1 (en) 1999-04-23 2008-08-12 Massachusetts Institute Of Technology Method for analyzing polysaccharides
AU4351201A (en) * 2000-03-08 2001-09-17 Massachusetts Inst Technology Heparinase iii and uses thereof
PT1319183E (en) 2000-09-12 2009-06-29 Massachusetts Inst Technology Methods and products related to low molecular weight heparin
AU2440802A (en) 2000-10-18 2002-04-29 Massachusetts Inst Technology Methods and products related to pulmonary delivery of polysaccharides
EP1575534B1 (en) * 2002-05-03 2013-04-10 Massachusetts Institute Of Technology D4,5 glycuronidase and uses thereof
EP2301564A1 (en) 2002-05-04 2011-03-30 Acorda Therapeutics, Inc. Compositions and methods for promoting neuronal outgrowth
WO2004055491A2 (en) * 2002-05-20 2004-07-01 Massachusetts Institute Of Technology Novel method for sequence determination using nmr
EP1532241B1 (en) * 2002-06-03 2010-09-15 Massachusetts Institute Of Technology Rationally designed polysaccharide lyases derived from chondroitinase b
ES2366333T3 (en) * 2002-08-15 2011-10-19 Acorda Therapeutics, Inc. CHEMICAL PROTEIN.
JP4606712B2 (en) * 2003-01-08 2011-01-05 マサチューセッツ インスティテュート オブ テクノロジー 2-O sulfatase compositions and related methods
EP3514238B1 (en) 2003-05-16 2021-05-05 Acorda Therapeutics, Inc. Proteoglycan degrading mutants for treatment of cns
US7959914B2 (en) 2003-05-16 2011-06-14 Acorda Therapeutics, Inc. Methods of reducing extravasation of inflammatory cells
ES2420510T3 (en) * 2003-05-16 2013-08-23 Acorda Therapeutics, Inc. Compositions and methods for the treatment of CNS lesions
AU2016204464B2 (en) * 2003-05-16 2018-03-22 Acorda Therapeutics, Inc. Proteoglycan degrading mutants for treatment of cns
WO2005000219A2 (en) * 2003-05-28 2005-01-06 The Board Of Trustees Of The University Of Illinois Composition for blocking hiv binding to dendritic cells and methods of use thereof
US7507570B2 (en) * 2004-03-10 2009-03-24 Massachusetts Institute Of Technology Recombinant chondroitinase ABC I and uses thereof
US20060127950A1 (en) 2004-04-15 2006-06-15 Massachusetts Institute Of Technology Methods and products related to the improved analysis of carbohydrates
US20060057638A1 (en) * 2004-04-15 2006-03-16 Massachusetts Institute Of Technology Methods and products related to the improved analysis of carbohydrates
WO2005110438A2 (en) * 2004-04-15 2005-11-24 Massachusetts Institute Of Technology Methods and products related to the intracellular delivery of polysaccharides
JP4926962B2 (en) 2004-05-18 2012-05-09 アコーダ セラピューティクス、インク． Purification method of chondroitinase and its stable preparation
EP1768687A2 (en) * 2004-06-29 2007-04-04 Massachusetts Institute Of Technology Methods and compositions related to the modulation of intercellular junctions
WO2006083328A2 (en) * 2004-09-15 2006-08-10 Massachusetts Institute Of Technology Biologically active surfaces and methods of their use
EP1928490B8 (en) 2005-09-26 2012-10-03 Acorda Therapeutics, Inc. Compositions and methods of using chondroitinase abci mutants
WO2007120478A2 (en) * 2006-04-03 2007-10-25 Massachusetts Institute Of Technology Glycomic patterns for the detection of disease
EP2450442B1 (en) 2006-10-10 2017-07-19 Acorda Therapeutics, Inc. Compositions and methods of using chondroitinase abci mutants
CA2674493C (en) 2007-01-05 2017-05-09 Massachusetts Institute Of Technology Compositions of and methods of using sulfatases from flavobacterium heparinum
EP2150616A4 (en) 2007-05-10 2011-07-27 Univ Arizona Regulated synthesis of antigen and/or regulated attentuation to enhance vaccine immunogenics and/or safety
GB0712302D0 (en) * 2007-06-22 2007-08-01 Cambridge Entpr Ltd Chrondroitinase polypeptides
US20090286289A1 (en) * 2008-03-10 2009-11-19 Pang Danny Z Production of Hyaluronate Unsaturated Disaccharides and its Application
US9045742B2 (en) * 2009-05-29 2015-06-02 The Arizona Board Of Regents For And On Behalf Of Arizona State University Recombinant Edwardsiella bacterium
US9796970B1 (en) 2017-04-24 2017-10-24 Advantek Serum Laboratories Ltd. Production of high purity chondroitinase ABC
CN111593040B (en) * 2020-06-20 2022-08-30 山东大学 Dermatan sulfate lyase and application thereof

Family Cites Families (75)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US197933A (en) * 1877-12-11 Improvement in wood-screws
US191587A (en) * 1877-06-05 Improvement in piano-forte bridges
US37376A (en) * 1863-01-06 Improvement in breech-loading fire-arms
US169143A (en) * 1875-10-26 Improvement in perforating stamps
US128225A (en) * 1872-06-25 Improvement in workmen s time-registers
US91472A (en) * 1869-06-15 Improvement in plows
US8820A (en) * 1852-03-23 Improvement in friction-primers for cannon
US92037A (en) * 1869-06-29 Improved shoe-pegging- machine
US204869A (en) * 1878-06-11 Improvement in weighing-scales
US99628A (en) * 1870-02-08 Signors to themselves and a
US122793A (en) * 1872-01-16 Improvement in air-supplying attachments for stoves
US91471A (en) * 1869-06-15 steigmeyer
JPS6031478B2 (en) 1978-02-10 1985-07-22 生化学工業株式会社 Method for producing pure chondroitinase B
US4341869A (en) * 1980-08-25 1982-07-27 Massachusetts Institute Of Technology Process for producing heparinase
US5169772A (en) * 1988-06-06 1992-12-08 Massachusetts Institute Of Technology Large scale method for purification of high purity heparinase from flavobacterium heparinum
JP2726275B2 (en) 1988-08-24 1998-03-11 生化学工業株式会社 Purification of glycosaminoglycan degrading enzyme
JPH0693836B2 (en) * 1988-11-25 1994-11-24 新技術事業団 Heparinase-producing microorganism belonging to the genus Bacillus, novel heparinase, and method for producing the same
ZA912770B (en) 1990-04-16 1992-01-29 Bethesda Eye Inst Enzymatic disinsertion of vitreous body
JPH04270327A (en) * 1991-02-26 1992-09-25 Fuji Photo Optical Co Ltd Exposure correcting device for camera
JP3110064B2 (en) * 1991-03-06 2000-11-20 生化学工業株式会社 Novel heparitinase, method for producing the same and bacteria producing the same
US5262325A (en) * 1991-04-04 1993-11-16 Ibex Technologies, Inc. Method for the enzymatic neutralization of heparin
US5668274A (en) 1991-04-23 1997-09-16 Akzo Nobel N.V. Sulfated glycosaminoglycanoid derivatives of the dermatan sulfate and chondroitin sulfate type
US5714376A (en) 1991-10-23 1998-02-03 Massachusetts Institute Of Technology Heparinase gene from flavobacterium heparinum
US6001630A (en) * 1992-06-26 1999-12-14 Seikagaku Kogyo Kabushiki Kaisha (Seikagaku Corporation) Pharmaceutical compositions of chondroitinase ABC isolated from Proteus vulgaris ATCC 6896
US5496718A (en) * 1992-06-26 1996-03-05 Seikagaku Kogyo Kabushiki Kaisha (Seikagaku Corporation) Chondroitinase ABC isolated from proteus vulgaris ATCC 6896
US5773277A (en) * 1992-06-26 1998-06-30 Seikagaku Kogyo Kabushiki Kaisha Crystalline chondroitinase isolated from Proteus vulgaris ATCC 6896
JP3419811B2 (en) 1993-02-24 2003-06-23 マルハ株式会社 Chondroitinase gene
US5389539A (en) * 1992-11-30 1995-02-14 Massachusetts Institute Of Technology Purification of heparinase I, II, and III from Flavobacterium heparinum
US5578480A (en) * 1993-04-23 1996-11-26 American Cyanamid Company Methods for the isolation and purification of the recombinantly expressed chondroitinase I and II enzymes from P. vulgaris
PL177218B1 (en) 1993-09-30 1999-10-29 Seikagaku Kogyo Co Ltd Anticoagulant
EP0726773A1 (en) 1993-11-17 1996-08-21 Massachusetts Institute Of Technology Method for inhibiting angiogenesis using heparinase
AU2428195A (en) 1994-04-22 1995-11-16 American Cyanamid Company Chondroitinases i and ii, methods of preparation, and use thereof
US5525500A (en) 1994-04-22 1996-06-11 American Cyanamid Company Chromatographic process for the copurification of chondroitinase I and II proteins from Proteus vulgaris
US5498536A (en) 1994-04-22 1996-03-12 American Cyanamid Company Chondroitinase II from Proteus vulgaris
US5681733A (en) * 1994-06-10 1997-10-28 Ibex Technologies Nucleic acid sequences and expression systems for heparinase II and heparinase III derived from Flavobacterium heparinum
US5619421A (en) * 1994-06-17 1997-04-08 Massachusetts Institute Of Technology Computer-implemented process and computer system for estimating the three-dimensional shape of a ring-shaped molecule and of a portion of a molecule containing a ring-shaped structure
US6093563A (en) 1994-07-08 2000-07-25 Ibex Technologies R And D, Inc. Chondroitin lyase enzymes
US5997863A (en) 1994-07-08 1999-12-07 Ibex Technologies R And D, Inc. Attenuation of wound healing processes
US5965507A (en) * 1995-06-08 1999-10-12 Procter & Gamble Company Cleaning compositions comprising chondroitinase
WO1997016556A1 (en) 1995-10-30 1997-05-09 Massachusetts Institute Of Technology Rationally designed polysaccharide lyases derived from heparinase i
US5866120A (en) * 1995-11-22 1999-02-02 Advanced Corneal Systems, Inc. Method for accelerating clearance of hemorrhagic blood from the vitreous humor with hyaluronidase
IT1285546B1 (en) 1996-01-16 1998-06-18 Alfa Wassermann Spa USE OF LOW MOLECULAR WEIGHT DERMATANE SULFATE AND MEDICINAL SPECIALTIES THAT CONTAIN IT IN THE THERAPY AND PREVENTION OF
DE69829605T2 (en) 1997-05-02 2006-02-09 Seikagaku Corp. Chondroitinase-containing compositions
DK0900569T3 (en) * 1997-08-22 2003-01-27 Seikagaku Kogyo Co Ltd Therapeutic agent for the treatment of herniaric intervertebral disc
US5968822A (en) * 1997-09-02 1999-10-19 Pecker; Iris Polynucleotide encoding a polypeptide having heparanase activity and expression of same in transduced cells
US6190875B1 (en) * 1997-09-02 2001-02-20 Insight Strategy & Marketing Ltd. Method of screening for potential anti-metastatic and anti-inflammatory agents using mammalian heparanase as a probe
US6378527B1 (en) * 1998-04-08 2002-04-30 Chondros, Inc. Cell-culture and polymer constructs
AU3985499A (en) 1998-05-13 1999-11-29 Biomarin Pharmaceutical Inc. Lytic enzymes useful for treating fungal infections
JP2000044601A (en) 1998-07-29 2000-02-15 Seikagaku Kogyo Co Ltd New galactosaminoglucan
US7412332B1 (en) 1999-04-23 2008-08-12 Massachusetts Institute Of Technology Method for analyzing polysaccharides
AU1608701A (en) 1999-11-12 2001-06-06 Biomarin Pharmaceutical Inc. Lytic enzymes useful for treating fungal infections
ATE413886T1 (en) 1999-11-17 2008-11-15 Biomarin Pharm Inc REDUCING ANGIOGENESIS USING CHONDROITIN SULPHATE DEGRADING ENZYMES
WO2001038399A1 (en) 1999-11-24 2001-05-31 Seikagaku Corporation Method of treating surface tissue diseases
JP2004504262A (en) 1999-12-02 2004-02-12 アイベックス　テクノロジーズ，　インコーポレイテッド Attenuated fibroblast proliferation
AU5790801A (en) 2000-01-21 2001-07-31 Biomarin Pharmaceutical Inc. Flavobacterium heparinum expression system
AU4351201A (en) 2000-03-08 2001-09-17 Massachusetts Inst Technology Heparinase iii and uses thereof
PT1319183E (en) 2000-09-12 2009-06-29 Massachusetts Inst Technology Methods and products related to low molecular weight heparin
AU2440802A (en) 2000-10-18 2002-04-29 Massachusetts Inst Technology Methods and products related to pulmonary delivery of polysaccharides
US20030008820A1 (en) 2001-03-27 2003-01-09 Massachusetts Institute Of Technology Methods and products related to FGF dimerization
CA2459040A1 (en) * 2001-09-14 2003-03-27 Mimeon, Inc. Methods of making glycolmolecules with enhanced activities and uses thereof
US20040214228A9 (en) * 2001-09-14 2004-10-28 Ganesh Venkataraman Methods of evaluating glycomolecules for enhanced activities
GB0205022D0 (en) 2002-03-04 2002-04-17 Univ Cambridge Tech Materials and methods for the treatment of cns damage
EP2284535A1 (en) * 2002-03-11 2011-02-16 Momenta Pharmaceuticals, Inc. Low molecular weight heparins
WO2003090696A2 (en) * 2002-04-25 2003-11-06 Momenta Pharmaceuticals, Inc. Methods and products for mucosal delivery
EP1575534B1 (en) * 2002-05-03 2013-04-10 Massachusetts Institute Of Technology D4,5 glycuronidase and uses thereof
WO2004055491A2 (en) 2002-05-20 2004-07-01 Massachusetts Institute Of Technology Novel method for sequence determination using nmr
EP1532241B1 (en) * 2002-06-03 2010-09-15 Massachusetts Institute Of Technology Rationally designed polysaccharide lyases derived from chondroitinase b
US20040147033A1 (en) * 2002-12-20 2004-07-29 Zachary Shriver Glycan markers for diagnosing and monitoring disease
JP4606712B2 (en) 2003-01-08 2011-01-05 マサチューセッツ インスティテュート オブ テクノロジー 2-O sulfatase compositions and related methods
KR100846449B1 (en) * 2003-03-27 2008-07-16 삼성전자주식회사 Method for setting web camera mode of mobile composition device
EP3514238B1 (en) 2003-05-16 2021-05-05 Acorda Therapeutics, Inc. Proteoglycan degrading mutants for treatment of cns
US7407810B2 (en) * 2003-09-04 2008-08-05 Momenta Pharmaceuticals, Inc. Methods and apparatus for characterizing polymeric mixtures
US7851223B2 (en) * 2004-02-27 2010-12-14 Roar Holding Llc Method to detect emphysema
CN101031287A (en) * 2004-03-02 2007-09-05 麻省理工学院 Nanocell drug delivery system
JP4926962B2 (en) 2004-05-18 2012-05-09 アコーダ セラピューティクス、インク． Purification method of chondroitinase and its stable preparation

Also Published As

Publication number Publication date
US7129335B2 (en) 2006-10-31
EP1532241A4 (en) 2005-12-14
US20070065424A1 (en) 2007-03-22
ATE481478T1 (en) 2010-10-15
US20040091472A1 (en) 2004-05-13
CA2493509C (en) 2010-03-09
WO2003102160A3 (en) 2004-09-16
AU2003243396A8 (en) 2003-12-19
US20050233419A1 (en) 2005-10-20
WO2003102160A2 (en) 2003-12-11
AU2003243396A1 (en) 2003-12-19
EP1532241B1 (en) 2010-09-15
US7105334B2 (en) 2006-09-12
EP1532241A2 (en) 2005-05-25
US6962699B2 (en) 2005-11-08
US20050227320A1 (en) 2005-10-13
DE60334220D1 (en) 2010-10-28

Similar Documents

Publication Publication Date Title
CA2493509A1 (en) Rationally designed polysaccharide lyases derived from chondroitinase b
JP5957096B2 (en) Bacillus, hyaluronic acid enzyme and use thereof
Wong et al. Alginate lyase: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
EP0487627B1 (en) Wound healing preparations containing heparanase
EP4015627B1 (en) Clostridium histolyticum enzyme
US9956273B2 (en) Compositions and methods for promoting neuronal outgrowth
CA2558984A1 (en) Recombinant chondroitinase abc i and uses thereof
JP2006504437A5 (en)
JP2004208684A5 (en)
CN107312765B (en) Glycosaminoglycan lyase and coding gene and application thereof
CN112126606B (en) Photobacterium QA16 and culture method and application thereof
CN111249302A (en) New application and stable manufacturing method of hyaluronic acid fragments
CN115521373B (en) Triple helix recombinant humanized type I collagen, preparation method and application thereof
Kale et al. Chondroitin lyase from a marine Arthrobacter sp. MAT3885 for the production of chondroitin sulfate disaccharides
CN109628347B (en) Photobacterium FC615 and culture method and application thereof
Sindelar et al. Hyaluronidases and hyaluronate lyases: From humans to bacteriophages
CN103923899B (en) A kind of glycosaminoglycan lyases and encoding gene and application
Stevens Secretory granule proteoglycans of mast cells and natural killer cells
Pang et al. Enzymatic production of low-molecular-weight hyaluronan and its oligosaccharides: A review and prospects
Watson et al. Characterization of a factor required for the differentiation of myeloid and lymphoid cells in vitro
Ennamany et al. SECMA 1®, a mitogenic hexapeptide from Ulva algeae modulates the production of proteoglycans and glycosaminoglycans in human foreskin fibroblast
CN111481660B (en) Pharmaceutical composition containing depolymerizing enzyme with function of degrading extracellular polymers of klebsiella pneumoniae
ES2617181T3 (en) Porphranases and their use to hydrolyze polysaccharides
WO2012136768A1 (en) Use of mutants of human hyaluronidase ph-20 with increased chondroitinase activity for axonal regrowth
CN112625139B (en) Protein and application thereof in promoting migration of skin fibroblasts, resisting bacteria and repairing wounds

Legal Events

Date Code Title Description
EEER Examination request
MKLA Lapsed

Effective date: 20210603