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Volumn 46, Issue 2, 2009, Pages 193-198

Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I

Author keywords

Affinity; Enzyme; Fusion protein; Heparinase; Low molecular weight heparin; Membrane; Stirred tank

Indexed keywords

AFFINITY; FUSION PROTEIN; HEPARINASE; LOW MOLECULAR WEIGHT HEPARIN; STIRRED-TANK;

EID: 67749130626     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2009.05.007     Document Type: Article
Times cited : (42)

References (20)
  • 1
    • 4644308426 scopus 로고    scopus 로고
    • Heparin and low-molecular-weight heparin-The Seventh ACCP Conference on Antithrombotic and Thrombolytic Therapy
    • Hirsh J., and Raschke R. Heparin and low-molecular-weight heparin-The Seventh ACCP Conference on Antithrombotic and Thrombolytic Therapy. Chest 126 (2004) 188s-203s
    • (2004) Chest , vol.126
    • Hirsh, J.1    Raschke, R.2
  • 2
    • 16644375606 scopus 로고    scopus 로고
    • Low doses and high doses of heparin have different effects on osteoblast-like Saos-2 cells in vitro
    • Hausser H.J., and Brenner R.E. Low doses and high doses of heparin have different effects on osteoblast-like Saos-2 cells in vitro. J. Cell Biochem. 91 (2004) 1062-1073
    • (2004) J. Cell Biochem. , vol.91 , pp. 1062-1073
    • Hausser, H.J.1    Brenner, R.E.2
  • 4
    • 54549100875 scopus 로고    scopus 로고
    • Preparation of LMWH and the relationship between its structure and bioactivity
    • Shi F., Ji S.L., Chi Y.Q., and Zhang T.M. Preparation of LMWH and the relationship between its structure and bioactivity. Chin. J. Biochem. Pharmaceut. 24 (2003) 101-104
    • (2003) Chin. J. Biochem. Pharmaceut. , vol.24 , pp. 101-104
    • Shi, F.1    Ji, S.L.2    Chi, Y.Q.3    Zhang, T.M.4
  • 5
    • 0032745131 scopus 로고    scopus 로고
    • Production and chemical processing of low molecular weight heparins
    • Linhardt R.J., and Gunay N.S. Production and chemical processing of low molecular weight heparins. Semin. Thromb. Hemost. 25 (1999) 5-16
    • (1999) Semin. Thromb. Hemost. , vol.25 , pp. 5-16
    • Linhardt, R.J.1    Gunay, N.S.2
  • 6
    • 52449122748 scopus 로고
    • Process of using light absorption to control enzymatic depolymerization of heparin to produce low molecular weight heparin,
    • US Patent 5106734
    • J.I. Nielsen, F. Denmark, Process of using light absorption to control enzymatic depolymerization of heparin to produce low molecular weight heparin, US Patent 5106734 (1992).
    • (1992)
    • Nielsen, J.I.1    Denmark, F.2
  • 7
    • 0033816137 scopus 로고    scopus 로고
    • Development of tinzaparin: a heparinase-digested low-molecular-weight heparin
    • Hedner U. Development of tinzaparin: a heparinase-digested low-molecular-weight heparin. Semin. Thromb. Hemost. 26 (2000) 23-29
    • (2000) Semin. Thromb. Hemost. , vol.26 , pp. 23-29
    • Hedner, U.1
  • 8
    • 0021920714 scopus 로고
    • Purification and characterization of heparinase from Flavobacterium heparinum
    • Yang V.C., Linhardt R.J., Bernstein H., Cooney C.L., and Langer R. Purification and characterization of heparinase from Flavobacterium heparinum. J. Biol. Chem. 260 (1985) 1849-1857
    • (1985) J. Biol. Chem. , vol.260 , pp. 1849-1857
    • Yang, V.C.1    Linhardt, R.J.2    Bernstein, H.3    Cooney, C.L.4    Langer, R.5
  • 9
    • 0026460982 scopus 로고
    • Purification and characterization of heparin lyase from Flavobacterium heparinum
    • Lohse D.L., and Linhardt R.J. Purification and characterization of heparin lyase from Flavobacterium heparinum. J. Biol. Chem. 276 (1992) 24347-24355
    • (1992) J. Biol. Chem. , vol.276 , pp. 24347-24355
    • Lohse, D.L.1    Linhardt, R.J.2
  • 10
    • 13244268462 scopus 로고    scopus 로고
    • Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein
    • Chen Y., Xing X.H., and Lou K. Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein. Biochem. Eng. J. 23 (2005) 155-159
    • (2005) Biochem. Eng. J. , vol.23 , pp. 155-159
    • Chen, Y.1    Xing, X.H.2    Lou, K.3
  • 11
    • 33947305443 scopus 로고    scopus 로고
    • Production of MBP-HepA fusion protein in recombinant Escherichia coli by optimization of culture medium
    • Chen Y., Xing X.H., Ye F.C., Kuang Y., and Luo M.F. Production of MBP-HepA fusion protein in recombinant Escherichia coli by optimization of culture medium. Biochem. Eng. J. 34 (2007) 114-121
    • (2007) Biochem. Eng. J. , vol.34 , pp. 114-121
    • Chen, Y.1    Xing, X.H.2    Ye, F.C.3    Kuang, Y.4    Luo, M.F.5
  • 12
    • 33750633211 scopus 로고    scopus 로고
    • Production of heparin oligosaccharides by fusion protein of MBP-heparinase I and the enzyme thermostability
    • Kuang Y., Xing X.H., Chen Y., Ye F.C., Yan Y.Y., Liu Z., and Bi R.C. Production of heparin oligosaccharides by fusion protein of MBP-heparinase I and the enzyme thermostability. J. Mol. Catal. B: Enzym. 43 (2006) 90-95
    • (2006) J. Mol. Catal. B: Enzym. , vol.43 , pp. 90-95
    • Kuang, Y.1    Xing, X.H.2    Chen, Y.3    Ye, F.C.4    Yan, Y.Y.5    Liu, Z.6    Bi, R.C.7
  • 13
    • 0028232767 scopus 로고
    • Feasibility study of heparin mass calibrator as a Gpc calibrator for heparins and low-molecular-weight heparins
    • Ahsan A., Jeske W., Mardiguian J., and Fareed J. Feasibility study of heparin mass calibrator as a Gpc calibrator for heparins and low-molecular-weight heparins. J. Pharm. Sci. 83 (1994) 197-201
    • (1994) J. Pharm. Sci. , vol.83 , pp. 197-201
    • Ahsan, A.1    Jeske, W.2    Mardiguian, J.3    Fareed, J.4
  • 14
    • 0033047666 scopus 로고    scopus 로고
    • Measurement of molecular weight and molecular weight distribution of low molecular weight heparin
    • Fan H.H., Liu J.X., and Xu K.S. Measurement of molecular weight and molecular weight distribution of low molecular weight heparin. Chin. Pharmaceut. J. 34 (1999) 332-334
    • (1999) Chin. Pharmaceut. J. , vol.34 , pp. 332-334
    • Fan, H.H.1    Liu, J.X.2    Xu, K.S.3
  • 16
    • 33744954960 scopus 로고    scopus 로고
    • Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product
    • Shaya D., Tocilj A., Li Y.G., Myette J., Venkataraman G., Sasisekharan R., and Cygler M. Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product. J. Biol. Chem. 281 (2006) 15525-15535
    • (2006) J. Biol. Chem. , vol.281 , pp. 15525-15535
    • Shaya, D.1    Tocilj, A.2    Li, Y.G.3    Myette, J.4    Venkataraman, G.5    Sasisekharan, R.6    Cygler, M.7
  • 17
    • 0025674559 scopus 로고
    • Randomness in the heparin polymer: computer simulations of alternative action patterns of heparin lyase
    • Cohen D.M., and Linhardt R.J. Randomness in the heparin polymer: computer simulations of alternative action patterns of heparin lyase. Biopolymers 30 (1990) 733-741
    • (1990) Biopolymers , vol.30 , pp. 733-741
    • Cohen, D.M.1    Linhardt, R.J.2
  • 18
    • 0028363168 scopus 로고
    • Action pattern of polysaccharide lyases on glycosaminoglycans
    • Jandik K.A., Gu K.A., and Linhardt R.J. Action pattern of polysaccharide lyases on glycosaminoglycans. Glycobiology 4 (1994) 289-296
    • (1994) Glycobiology , vol.4 , pp. 289-296
    • Jandik, K.A.1    Gu, K.A.2    Linhardt, R.J.3
  • 19
    • 0031002162 scopus 로고    scopus 로고
    • A unique trisaccharide sequence in heparin mediates the early step of antithrombin III activation
    • Petitiou M., Barzu T., and Herault J.P. A unique trisaccharide sequence in heparin mediates the early step of antithrombin III activation. Glycobiology 7 (1997) 323-327
    • (1997) Glycobiology , vol.7 , pp. 323-327
    • Petitiou, M.1    Barzu, T.2    Herault, J.P.3
  • 20
    • 0019801543 scopus 로고
    • The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence
    • Casu B., and Oreste P. The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence. Biochem. J. 97 (1981) 599-609
    • (1981) Biochem. J. , vol.97 , pp. 599-609
    • Casu, B.1    Oreste, P.2


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