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Volumn 26, Issue 1-2, 2009, Pages 99-104

Rapid purification and characterization of a novel heparin degrading enzyme from Acinetobacter calcoaceticus

Author keywords

[No Author keywords available]

Indexed keywords

ACINETOBACTER CALCOACETICUS; ACINETOBACTERS; CATALYTIC ACTIVITY; CYSTEINE RESIDUES; DEGRADING ENZYMES; G PROTEIN; GEL-FILTRATION CHROMATOGRAPHY; GLYCOSAMINOGLYCANS; HEPARIN DISACCHARIDE; HIGH AFFINITY; IN-SITU; IODOACETIC ACID; PERIPLASMIC SPACE; PURIFIED ENZYME; PURIFIED PROTEIN; RAPID PURIFICATION; SPECIFIC ACTIVITY;

EID: 71749091821     PISSN: 18716784     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbt.2009.04.003     Document Type: Article
Times cited : (6)

References (27)
  • 1
    • 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 Suppl. 3 (1999) 5-16
    • (1999) Semin. Thromb. Hemost. , vol.25 , Issue.SUPPL. 3 , pp. 5-16
    • Linhardt, R.J.1    Gunay, N.S.2
  • 2
    • 0034641723 scopus 로고    scopus 로고
    • Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin
    • Shriver Z., et al. Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 10365-10370
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10365-10370
    • Shriver, Z.1
  • 3
    • 1842463681 scopus 로고    scopus 로고
    • Antimetastatic effect of tinzaparin, a low-molecular-weight heparin
    • Amirkhosravi A., et al. Antimetastatic effect of tinzaparin, a low-molecular-weight heparin. J. Thromb. Haemost. 1 (2003) 1972-1976
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1972-1976
    • Amirkhosravi, A.1
  • 4
    • 0034326271 scopus 로고    scopus 로고
    • Unfractionated and low molecular weight heparin affect fibrin structure and angiogenesis in vitro
    • Collen A., et al. Unfractionated and low molecular weight heparin affect fibrin structure and angiogenesis in vitro. Cancer Res. 60 (2000) 6196-6200
    • (2000) Cancer Res. , vol.60 , pp. 6196-6200
    • Collen, A.1
  • 5
    • 0018605698 scopus 로고
    • Heparin: an old drug with a new paradigm
    • Jacques L.B. Heparin: an old drug with a new paradigm. Science 206 (1979) 528-533
    • (1979) Science , vol.206 , pp. 528-533
    • Jacques, L.B.1
  • 6
    • 71749107488 scopus 로고
    • Fractionated heparin for the therapeutic treatment of malaria
    • US Patent 5,472,953
    • Wahlin, B. et al. (1995) Fractionated heparin for the therapeutic treatment of malaria. US Patent 5,472,953
    • (1995)
    • Wahlin, B.1
  • 7
    • 0028013669 scopus 로고
    • Heparinase inhibits neovascularization
    • Sasisekharan R., et al. Heparinase inhibits neovascularization. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 1524-1528
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1524-1528
    • Sasisekharan, R.1
  • 8
    • 71749090968 scopus 로고    scopus 로고
    • Heparinase III and uses thereof
    • EP Patent 1,266,013
    • Dongfang, L. et al. (2002) Heparinase III and uses thereof. EP Patent 1,266,013
    • (2002)
    • Dongfang, L.1
  • 9
    • 0027209887 scopus 로고
    • Enzymatic elimination of heparin from plasma for activated partial thromboplastin time and prothrombin time testing
    • van den Besselaar A., and Meeuwisse-Braun J. Enzymatic elimination of heparin from plasma for activated partial thromboplastin time and prothrombin time testing. Blood Coagul. Fibrinolysis. 4 (1993) 635
    • (1993) Blood Coagul. Fibrinolysis. , vol.4 , pp. 635
    • van den Besselaar, A.1    Meeuwisse-Braun, J.2
  • 10
    • 1842347492 scopus 로고
    • Method for the enzymatic neutralization of heparin
    • US Patent 5,262,325
    • Zimmerman, J. et al. (1993) Method for the enzymatic neutralization of heparin. US Patent 5,262,325
    • (1993)
    • Zimmerman, J.1
  • 11
    • 0026460982 scopus 로고
    • Purification and characterization of heparin lyases from Flavobacterium heparinum
    • Lohse D., and Linhardt R. Purification and characterization of heparin lyases from Flavobacterium heparinum. J. Biol. Chem. 267 (1992) 24347-24355
    • (1992) J. Biol. Chem. , vol.267 , pp. 24347-24355
    • Lohse, D.1    Linhardt, R.2
  • 12
    • 0142121657 scopus 로고    scopus 로고
    • Rapid purification, characterization and substrate specificity of heparinase from a novel species of Sphingobacterium
    • Yapeng C., et al. Rapid purification, characterization and substrate specificity of heparinase from a novel species of Sphingobacterium. J. Biochem. 134 (2003) 365-371
    • (2003) J. Biochem. , vol.134 , pp. 365-371
    • Yapeng, C.1
  • 13
    • 0036560772 scopus 로고    scopus 로고
    • Purification and characterization of heparinase that degrades both heparin and heparan sulfate from Bacillus circulans
    • Yoshida E., et al. Purification and characterization of heparinase that degrades both heparin and heparan sulfate from Bacillus circulans. Biosci. Biotechnol. Biochem. 66 (2002) 1181-1184
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1181-1184
    • Yoshida, E.1
  • 14
    • 13544265550 scopus 로고    scopus 로고
    • Purification and characterization of heparin lyase I from Bacteroides stercoris HJ-15
    • Kim W.S., et al. Purification and characterization of heparin lyase I from Bacteroides stercoris HJ-15. J. Biochem. Mol. Biol. 37 (2004) 684-690
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 684-690
    • Kim, W.S.1
  • 15
    • 0030840750 scopus 로고    scopus 로고
    • Phylogenetic relationship of the twenty-one DNA groups of the genus Acinetobacter as revealed by 16S ribosomal DNA sequence analysis
    • Ibrahim A., et al. Phylogenetic relationship of the twenty-one DNA groups of the genus Acinetobacter as revealed by 16S ribosomal DNA sequence analysis. Int. J. Syst. Evol. Microbiol. 47 (1997) 837-841
    • (1997) Int. J. Syst. Evol. Microbiol. , vol.47 , pp. 837-841
    • Ibrahim, A.1
  • 16
    • 3042950135 scopus 로고
    • Freeze-thawing of Aquaspirillum magnetotacticum cells selectively releases periplasmic proteins
    • Paoletti L.C., et al. Freeze-thawing of Aquaspirillum magnetotacticum cells selectively releases periplasmic proteins. Appl. Environ. Microbiol. 53 (1987) 2590-2592
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2590-2592
    • Paoletti, L.C.1
  • 17
    • 0001212573 scopus 로고
    • Heparinase and heparitinase from flavo-bacteria
    • Ginsburg U. (Ed), Academic Press
    • Linker A., and Hovingh P. Heparinase and heparitinase from flavo-bacteria. In: Ginsburg U. (Ed). Methods in Enzymology (1972), Academic Press 902-911
    • (1972) Methods in Enzymology , pp. 902-911
    • Linker, A.1    Hovingh, P.2
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O.H., et al. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld J., et al. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203 (1992) 173-179
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1
  • 21
    • 71749095080 scopus 로고    scopus 로고
    • Sasisekharan, R. et al. (1996) Purification, composition and specificity of heparinase I, II, and III from flavobacterium heparinum. US Patent 5,569,600
    • Sasisekharan, R. et al. (1996) Purification, composition and specificity of heparinase I, II, and III from flavobacterium heparinum. US Patent 5,569,600
  • 22
    • 0043196405 scopus 로고
    • Heparinase produced by microorganism belonging to the genus bacillus
    • US Patent 5,145,778
    • Bellamy, R. and Horikoshi, K. (1992) Heparinase produced by microorganism belonging to the genus bacillus. US Patent 5,145,778
    • (1992)
    • Bellamy, R.1    Horikoshi, K.2
  • 23
    • 0031972599 scopus 로고    scopus 로고
    • Heparinase I from Flavobacterium heparinum. Role of positive charge in enzymatic activity
    • Godavarti R., and Sasisekharan R. Heparinase I from Flavobacterium heparinum. Role of positive charge in enzymatic activity. J. Biol. Chem. 273 (1998) 248-255
    • (1998) J. Biol. Chem. , vol.273 , pp. 248-255
    • Godavarti, R.1    Sasisekharan, R.2
  • 24
    • 0032483440 scopus 로고    scopus 로고
    • Heparinase II from Flavobacterium heparinum. Role of cysteine in enzymatic activity as probed by chemical modification and site- directed mutagenesis
    • Shriver Z., et al. Heparinase II from Flavobacterium heparinum. Role of cysteine in enzymatic activity as probed by chemical modification and site- directed mutagenesis. J. Biol. Chem. 273 (1998) 22904-22912
    • (1998) J. Biol. Chem. , vol.273 , pp. 22904-22912
    • Shriver, Z.1
  • 25
    • 33744954960 scopus 로고    scopus 로고
    • Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product
    • Shaya D., et al. 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
  • 26
    • 0023654989 scopus 로고
    • Fractionation of heparin-derived oligosaccharides by gradient polyacrylamide-gel electrophoresis
    • Rice K.G., et al. Fractionation of heparin-derived oligosaccharides by gradient polyacrylamide-gel electrophoresis. Biochem. J. 244 (1987) 515-522
    • (1987) Biochem. J. , vol.244 , pp. 515-522
    • Rice, K.G.1
  • 27
    • 71749091390 scopus 로고    scopus 로고
    • Oligosaccharides, preparation method and use thereof, and pharmaceutical compositions containing same
    • US patent 0,142,323
    • Viskov, C. and Mourier, P. (2007) Oligosaccharides, preparation method and use thereof, and pharmaceutical compositions containing same. US patent 0,142,323
    • (2007)
    • Viskov, C.1    Mourier, P.2


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