메뉴 건너뛰기




Volumn 92, Issue , 2015, Pages 257-269

Anticoagulant and antithrombotic evaluation of native fucosylated chondroitin sulfates and their derivatives as selective inhibitors of intrinsic factor Xase

Author keywords

Anticoagulant; Antithrombotic; Factor Xase inhibitor; Fucosylated chondroitin sulfate; Structureeactivity relationship

Indexed keywords

ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 12; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 8A; BLOOD CLOTTING FACTOR 9A; CARBOHYDRATE; CARBOXYL GROUP; FUCOSYLATED CHONDROITIN SULFATE; FUCOSYLATED CHONDROITIN SULFATE DERIVATIVE; GLYCOSAMINOGLYCAN; INTRINSIC FACTOR; TRISACCHARIDE; UNCLASSIFIED DRUG; CHONDROITIN SULFATE; CYSTEINE PROTEINASE; ENZYME INHIBITOR; FIBRINOLYTIC AGENT;

EID: 84920160745     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2014.12.054     Document Type: Article
Times cited : (112)

References (52)
  • 2
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions: Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • S.T. Olson, I. Bjork, R. Sheffer, P.A. Craig, J.D. Shore, J. Choay, Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions: resolution of the antithrombin conformational change contribution to heparin rate enhancement, J. Biol. Chem. 267 (1992) 12528-12538.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 3
    • 0001668795 scopus 로고
    • Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin
    • U. Lindahl, G. Backstrom, L. Thunberg, I.G. Leder, Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin, Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 6551-6555.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6551-6555
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3    Leder, I.G.4
  • 5
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin
    • W. Li, D.J. Johnson, C.T. Esmon, J.A. Huntington, Structure of the antithrombin thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin, Nat. Struct. Mol. Biol. 11 (2004) 857-862.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 857-862
    • Li, W.1    Johnson, D.J.2    Esmon, C.T.3    Huntington, J.A.4
  • 6
    • 0030858861 scopus 로고    scopus 로고
    • The anticoagulant and hemorrhagic effects of DHG, a new depolymerized holothurian glycosaminoglycan, on experimental hemodialysis in dogs
    • K. Minamiguchi, K.T. Kitazato, E. Sasaki, H. Nagase, K. Kitazato, The anticoagulant and hemorrhagic effects of DHG, a new depolymerized holothurian glycosaminoglycan, on experimental hemodialysis in dogs, Thromb. Haemost. 77 (1997) 1148-1153.
    • (1997) Thromb. Haemost. , vol.77 , pp. 1148-1153
    • Minamiguchi, K.1    Kitazato, K.T.2    Sasaki, E.3    Nagase, H.4    Kitazato, K.5
  • 9
    • 0029858330 scopus 로고    scopus 로고
    • Blood clotting in minimally altered whole blood
    • M.D. Rand, J.B. Lock, C. Veer, D.P. Gaffney, K.G. Mann, Blood clotting in minimally altered whole blood, Blood 88 (1996) 3432-3445.
    • (1996) Blood , vol.88 , pp. 3432-3445
    • Rand, M.D.1    Lock, J.B.2    Veer, C.3    Gaffney, D.P.4    Mann, K.G.5
  • 10
    • 0037166290 scopus 로고    scopus 로고
    • A model for the stoichiometric regulation of blood coagulation
    • M.F. Hockin, K.C. Jones, S.J. Everse, K.G. Mann, A model for the stoichiometric regulation of blood coagulation, J. Biol. Chem. 277 (2002) 18322-18333.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18322-18333
    • Hockin, M.F.1    Jones, K.C.2    Everse, S.J.3    Mann, K.G.4
  • 11
    • 33646543029 scopus 로고    scopus 로고
    • Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin independent mechanism
    • J.P. Sheehan, E.N. Walke, Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin independent mechanism, Blood 107 (2006) 3876-3882.
    • (2006) Blood , vol.107 , pp. 3876-3882
    • Sheehan, J.P.1    Walke, E.N.2
  • 12
    • 84892865069 scopus 로고    scopus 로고
    • Holothurian fucosylated chondroitin sulfate
    • V.H. Pomin, Holothurian fucosylated chondroitin sulfate, Mar. Drugs 12 (2014) 232-254.
    • (2014) Mar. Drugs , vol.12 , pp. 232-254
    • Pomin, V.H.1
  • 13
    • 0025780346 scopus 로고
    • Antithrombotic and anticoagulant activity of depolymerized fragment of the glycosaminoglycan extracted from Stichopus japonicus Selenka
    • N. Suzuki, K. Kitazato, J. Takamatsu, H. Saito, Antithrombotic and anticoagulant activity of depolymerized fragment of the glycosaminoglycan extracted from Stichopus japonicus Selenka, Thromb. Haemost. 65 (1991) 369-373.
    • (1991) Thromb. Haemost. , vol.65 , pp. 369-373
    • Suzuki, N.1    Kitazato, K.2    Takamatsu, J.3    Saito, H.4
  • 14
    • 0029796369 scopus 로고    scopus 로고
    • Structure and anticoagulant activity of a fucosylated chondroitin sulfate from echinoderm: Sulfated fucose branches on the polysaccharide account for its high anticoagulant action
    • P.A.S. Mourão, M.S. Pereira, M.S.G. Pavão, B. Mulloy, D.M. Tollefsen, M.C. Mowinckel, U. Abildgaard, Structure and anticoagulant activity of a fucosylated chondroitin sulfate from echinoderm: sulfated fucose branches on the polysaccharide account for its high anticoagulant action, J. Biol. Chem. 271 (1996) 23973-23984.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23973-23984
    • Mourão, P.A.S.1    Pereira, M.S.2    Pavão, M.S.G.3    Mulloy, B.4    Tollefsen, D.M.5    Mowinckel, M.C.6    Abildgaard, U.7
  • 15
    • 84875769078 scopus 로고    scopus 로고
    • Comparison of physicochemical characteristics and anticoagulant activities of polysaccharides from three sea cucumbers
    • L. Luo, M. Wu, L. Xu, W. Lian, J. Xiang, F. Lu, N. Gao, C. Xiao, S. Wang, J. Zhao, Comparison of physicochemical characteristics and anticoagulant activities of polysaccharides from three sea cucumbers, Mar. Drugs 11 (2013) 399-417.
    • (2013) Mar. Drugs , vol.11 , pp. 399-417
    • Luo, L.1    Wu, M.2    Xu, L.3    Lian, W.4    Xiang, J.5    Lu, F.6    Gao, N.7    Xiao, C.8    Wang, S.9    Zhao, J.10
  • 16
    • 0028921935 scopus 로고
    • Depolymerized holothurian glycosaminoglycan with novel anticoagulant actions: Antithrombin III-and heparin cofactor II-independent inhibition of factor X activation by factor IXa-factor VIIIa complex and heparin cofactor IIdependent inhibition of thrombin
    • H. Nagase, K. Enjyoji, K. Minamiguchi, K. Kitazato, H. Saito, H. Kato, Depolymerized holothurian glycosaminoglycan with novel anticoagulant actions: antithrombin III-and heparin cofactor II-independent inhibition of factor X activation by factor IXa-factor VIIIa complex and heparin cofactor IIdependent inhibition of thrombin, Blood 85 (1995) 1527-1534.
    • (1995) Blood , vol.85 , pp. 1527-1534
    • Nagase, H.1    Enjyoji, K.2    Minamiguchi, K.3    Kitazato, K.4    Saito, H.5    Kato, H.6
  • 17
    • 0033833568 scopus 로고    scopus 로고
    • Different antithrombotic mechanisms among glycosaminoglycans revealed with a new fucosylated chondroitin sulfate from an echinoderm
    • R.G. Pacheco, C.P. Vicente, P. Zancan, P.A.S. Mourão, Different antithrombotic mechanisms among glycosaminoglycans revealed with a new fucosylated chondroitin sulfate from an echinoderm, Blood Coagul. Fibrinolysis 11 (2000) 563-573.
    • (2000) Blood Coagul. Fibrinolysis , vol.11 , pp. 563-573
    • Pacheco, R.G.1    Vicente, C.P.2    Zancan, P.3    Mourão, P.A.S.4
  • 18
    • 80054745034 scopus 로고    scopus 로고
    • Structure and effect of sulfated fucose branches on anticoagulant activity of the fucosylated chondroitin sulfate from sea cucumber Thelenata ananas
    • M. Wu, R. Huang, D. Wen, N. Gao, J. He, Z. Li, J. Zhao, Structure and effect of sulfated fucose branches on anticoagulant activity of the fucosylated chondroitin sulfate from sea cucumber Thelenata ananas, Carbohydr. Polym. 87 (2012) 862-868.
    • (2012) Carbohydr. Polym. , vol.87 , pp. 862-868
    • Wu, M.1    Huang, R.2    Wen, D.3    Gao, N.4    He, J.5    Li, Z.6    Zhao, J.7
  • 19
    • 0030025579 scopus 로고    scopus 로고
    • Effect of depolymerized holothurian glycosaminoglycan (DHG) on the activation of factor VIII and factor v by thrombin
    • H. Nagase, K. Enjyoji, M. Shima, K. Kitazato, A. Yoshioka, H. Saito, H. Kato, Effect of depolymerized holothurian glycosaminoglycan (DHG) on the activation of factor VIII and factor V by thrombin, J. Biochem. 119 (1996) 63-69.
    • (1996) J. Biochem. , vol.119 , pp. 63-69
    • Nagase, H.1    Enjyoji, K.2    Shima, M.3    Kitazato, K.4    Yoshioka, A.5    Saito, H.6    Kato, H.7
  • 20
    • 51349116958 scopus 로고    scopus 로고
    • Serpin-independent anticoagulant activity of a fucosylated chondroitin sulfate
    • B.F. Glauser, M.S. Pereira, R.Q. Monteiro, P.A.S. Mourão, Serpin-independent anticoagulant activity of a fucosylated chondroitin sulfate, Thromb. Haemost. 100 (2008) 420-428.
    • (2008) Thromb. Haemost. , vol.100 , pp. 420-428
    • Glauser, B.F.1    Pereira, M.S.2    Monteiro, R.Q.3    Mourão, P.A.S.4
  • 21
    • 70449464372 scopus 로고    scopus 로고
    • Fucosylated chondroitin sulfate inhibits plasma thrombin generation via targeting of the factor IXa heparin-binding exosite
    • Y. Buyue, J.P. Sheehan, Fucosylated chondroitin sulfate inhibits plasma thrombin generation via targeting of the factor IXa heparin-binding exosite, Blood 114 (2009) 3092-3100.
    • (2009) Blood , vol.114 , pp. 3092-3100
    • Buyue, Y.1    Sheehan, J.P.2
  • 22
    • 0031058101 scopus 로고    scopus 로고
    • Antithrombin III-independent effect of depolymerized holothurian glycosaminoglycan (DHG) on acute thromboembolism in mice
    • H. Nagase, K.T. Kitazato, E. Sasaki, M. Hattori, K. Kitazato, H. Saito, Antithrombin III-independent effect of depolymerized holothurian glycosaminoglycan (DHG) on acute thromboembolism in mice, Thromb. Haemost. 77 (1997) 399-402.
    • (1997) Thromb. Haemost. , vol.77 , pp. 399-402
    • Nagase, H.1    Kitazato, K.T.2    Sasaki, E.3    Hattori, M.4    Kitazato, K.5    Saito, H.6
  • 23
    • 0031831742 scopus 로고    scopus 로고
    • Antithrombotic activity of a fucosylated chondroitin sulphate from echinoderm: Sulphated fucose branches on the polysaccharide account for its antithrombotic action
    • P.A.S. Mourão, M.A.M. Guimarães, B. Mulloy, S. Thomas, E. Gray, Antithrombotic activity of a fucosylated chondroitin sulphate from echinoderm: sulphated fucose branches on the polysaccharide account for its antithrombotic action, Br. J. Haematol. 101 (1998) 647-652.
    • (1998) Br. J. Haematol. , vol.101 , pp. 647-652
    • Mourão, P.A.S.1    Guimarães, M.A.M.2    Mulloy, B.3    Thomas, S.4    Gray, E.5
  • 24
    • 70449581263 scopus 로고    scopus 로고
    • Effects of polysaccharides enriched in 2,4-disulfated fucose units on coagulation, thrombosis and bleeding. Practical and conceptual implications
    • R.J. Fonseca, G.R. Santos, P.A.S. Mourão, Effects of polysaccharides enriched in 2,4-disulfated fucose units on coagulation, thrombosis and bleeding. Practical and conceptual implications, Thromb. Haemost. 102 (2009) 829-836.
    • (2009) Thromb. Haemost. , vol.102 , pp. 829-836
    • Fonseca, R.J.1    Santos, G.R.2    Mourão, P.A.S.3
  • 25
    • 0023878541 scopus 로고
    • Mechanism of rabbit platelet agglutination induced by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka
    • J.Z. Li, E.C. Lian, Mechanism of rabbit platelet agglutination induced by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka, Thromb. Haemost. 59 (1988) 432-434.
    • (1988) Thromb. Haemost. , vol.59 , pp. 432-434
    • Li, J.Z.1    Lian, E.C.2
  • 26
    • 0030588206 scopus 로고    scopus 로고
    • DHG, a new depolymerized holothurian glycosaminoglycan, exerts an antithrombotic effect with less bleeding than unfractionated or low molecular weight heparin, in rats
    • K. Kitazato, K.T. Kitazato, H. Nagase, K. Minamiguchi, DHG, a new depolymerized holothurian glycosaminoglycan, exerts an antithrombotic effect with less bleeding than unfractionated or low molecular weight heparin, in rats, Thromb. Res. 84 (1996) 111-120.
    • (1996) Thromb. Res. , vol.84 , pp. 111-120
    • Kitazato, K.1    Kitazato, K.T.2    Nagase, H.3    Minamiguchi, K.4
  • 27
    • 0842281338 scopus 로고    scopus 로고
    • Prolonged bleeding time induced by anticoagulant glycosaminoglycans in dogs is associated with the inhibition of thrombin-induced platelet aggregation
    • K. Kitazato, K.T. Kitazato, E. Sasaki, K. Minamiguchi, H. Nagase, Prolonged bleeding time induced by anticoagulant glycosaminoglycans in dogs is associated with the inhibition of thrombin-induced platelet aggregation, Thromb. Res. 112 (2003) 83-91.
    • (2003) Thromb. Res. , vol.112 , pp. 83-91
    • Kitazato, K.1    Kitazato, K.T.2    Sasaki, E.3    Minamiguchi, K.4    Nagase, H.5
  • 28
    • 0023875679 scopus 로고
    • Aggregation of human platelets by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka
    • J.Z. Li, E.C. Lian, Aggregation of human platelets by acidic mucopolysaccharide extracted from Stichopus japonicus Selenka, Thromb. Haemost. 59 (1988) 435-439.
    • (1988) Thromb. Haemost. , vol.59 , pp. 435-439
    • Li, J.Z.1    Lian, E.C.2
  • 29
    • 77952087454 scopus 로고    scopus 로고
    • Effects of oversulfated and fucosylated chondroitin sulfates on coagulation. Challenges for the study of anticoagulant polysaccharides
    • R.J. Fonseca, S.N. Oliveira, V.H. Pomin, A.S. Mecawi, I.G. Araujo, P.A.S. Mourão, Effects of oversulfated and fucosylated chondroitin sulfates on coagulation. Challenges for the study of anticoagulant polysaccharides, Thromb. Haemost. 103 (2010) 994-1004.
    • (2010) Thromb. Haemost. , vol.103 , pp. 994-1004
    • Fonseca, R.J.1    Oliveira, S.N.2    Pomin, V.H.3    Mecawi, A.S.4    Araujo, I.G.5    Mourão, P.A.S.6
  • 30
    • 78349310561 scopus 로고    scopus 로고
    • Comparison of structures and anticoagulant activities of fucosylated chondroitin sulfates from different sea cucumbers
    • S. Chen, C. Xue, L. Yin, Q. Tang, G. Yu, W. Chai, Comparison of structures and anticoagulant activities of fucosylated chondroitin sulfates from different sea cucumbers, Carbohydr. Polym. 83 (2011) 688-696.
    • (2011) Carbohydr. Polym. , vol.83 , pp. 688-696
    • Chen, S.1    Xue, C.2    Yin, L.3    Tang, Q.4    Yu, G.5    Chai, W.6
  • 31
    • 77951628214 scopus 로고    scopus 로고
    • Physicochemical characteristics and anticoagulant activities of low molecular weight fractions by free radical depolymerization of a fucosylated chondroitin sulfate from sea cucumber Thelenota ananas
    • M. Wu, S. Xu, J. Zhao, H. Kang, H. Ding, Physicochemical characteristics and anticoagulant activities of low molecular weight fractions by free radical depolymerization of a fucosylated chondroitin sulfate from sea cucumber Thelenota ananas, Food Chem. 122 (2010) 716-723.
    • (2010) Food Chem. , vol.122 , pp. 716-723
    • Wu, M.1    Xu, S.2    Zhao, J.3    Kang, H.4    Ding, H.5
  • 32
    • 0035043554 scopus 로고    scopus 로고
    • Determination of the molecular mass of new L-fucose-containing glycosaminoglycan and its distribution by high-performance gel-permeation chromatography with laser lightscattering detection
    • T. Tsukamoto, M. Hattori, M. Sakabe, J. Haginaka, Determination of the molecular mass of new L-fucose-containing glycosaminoglycan and its distribution by high-performance gel-permeation chromatography with laser lightscattering detection, Anal. Sci. 17 (2001) 555-558.
    • (2001) Anal. Sci. , vol.17 , pp. 555-558
    • Tsukamoto, T.1    Hattori, M.2    Sakabe, M.3    Haginaka, J.4
  • 33
    • 0026670983 scopus 로고
    • Structure of DHG, a depolymerized glycosaminoglycan from sea cucumber, Stichopus japonicas
    • K. Yoshida, Y. Minami, H. Nemoto, K. Numata, E. Yamanaka, Structure of DHG, a depolymerized glycosaminoglycan from sea cucumber, Stichopus japonicas, Tetrahedron Lett. 33 (1992) 4959-4962.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 4959-4962
    • Yoshida, K.1    Minami, Y.2    Nemoto, H.3    Numata, K.4    Yamanaka, E.5
  • 35
    • 0026575370 scopus 로고
    • Low molecular weight heparins (5 kDa) and oligoheparins (2 kDa) produced by gel permeation enrichment or radical process: Comparison of structures and physicochemical and biological properties
    • N. Volpi, G. Mascellani, P. Bianchini, Low molecular weight heparins (5 kDa) and oligoheparins (2 kDa) produced by gel permeation enrichment or radical process: comparison of structures and physicochemical and biological properties, Anal. Biochem. 200 (1992) 100-107.
    • (1992) Anal. Biochem. , vol.200 , pp. 100-107
    • Volpi, N.1    Mascellani, G.2    Bianchini, P.3
  • 37
    • 65749088905 scopus 로고    scopus 로고
    • Oversulfated chondroitin sulfate interaction with heparinbinding proteins: New insights into adverse reactions from contaminated heparins
    • B. Li, J. Suwan, J.G. Martin, Z. Zhang, D. Hoppensteadt, M. Clark, J. Fareed, R.J. Linhardt, Oversulfated chondroitin sulfate interaction with heparinbinding proteins: new insights into adverse reactions from contaminated heparins, Biochem. Pharmacol. 78 (2009) 292-300.
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 292-300
    • Li, B.1    Suwan, J.2    Martin, J.G.3    Zhang, Z.4    Hoppensteadt, D.5    Clark, M.6    Fareed, J.7    Linhardt, R.J.8
  • 38
    • 0023547622 scopus 로고
    • The autoactivation of factor XII (hageman factor) induced by low-Mr heparin and dextran sulphate: The effect of the Mr of the activating polyanion
    • S. Michael, V.D. Susan, The autoactivation of factor XII (hageman factor) induced by low-Mr heparin and dextran sulphate: the effect of the Mr of the activating polyanion, Biochem. J. 248 (1987) 715-720.
    • (1987) Biochem. J. , vol.248 , pp. 715-720
    • Michael, S.1    Susan, V.D.2
  • 39
    • 0019499060 scopus 로고
    • The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin
    • E. Holmer, K. Kurachi, G. Söderström, The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin, Biochem. J. 193 (1981) 395-400.
    • (1981) Biochem. J. , vol.193 , pp. 395-400
    • Holmer, E.1    Kurachi, K.2    Söderström, G.3
  • 40
    • 0033599835 scopus 로고    scopus 로고
    • New antithrombotic agents
    • J. Hirsh, J.I. Weitz, New antithrombotic agents, Lancet 353 (1999) 1431-1436.
    • (1999) Lancet , vol.353 , pp. 1431-1436
    • Hirsh, J.1    Weitz, J.I.2
  • 41
    • 0032505019 scopus 로고    scopus 로고
    • Low-molecularweight heparins: Pharmacologic profile and product differentiation
    • J. Fareed, W. Jeske, D. Hoppensteadt, R. Clarizio, J.M. Walenga, Low-molecularweight heparins: pharmacologic profile and product differentiation, Am. J. Cardiol. 82 (1998) 3Le10L.
    • (1998) Am. J. Cardiol. , vol.82 , pp. 3Le10L
    • Fareed, J.1    Jeske, W.2    Hoppensteadt, D.3    Clarizio, R.4    Walenga, J.M.5
  • 42
    • 12444322508 scopus 로고
    • Heparin derivatives prepared by modification of the uronic carboxyl groups
    • I. Danishefsky, E. Siskovic, Heparin derivatives prepared by modification of the uronic carboxyl groups, Thromb. Res. 1 (1972) 173-182.
    • (1972) Thromb. Res. , vol.1 , pp. 173-182
    • Danishefsky, I.1    Siskovic, E.2
  • 43
    • 84882765904 scopus 로고    scopus 로고
    • Structure and anticoagulant activity of fucosylated glycosaminoglycan degraded by deaminative cleavage
    • L.Y. Zhao, S.S. Lai, R. Huang, M.Y. Wu, N. Gao, L. Xu, H.B. Qin, W.L. Peng, J.H. Zhao, Structure and anticoagulant activity of fucosylated glycosaminoglycan degraded by deaminative cleavage, Carbohydr. Polym. 98 (2013) 1514-1523.
    • (2013) Carbohydr. Polym. , vol.98 , pp. 1514-1523
    • Zhao, L.Y.1    Lai, S.S.2    Huang, R.3    Wu, M.Y.4    Gao, N.5    Xu, L.6    Qin, H.B.7    Peng, W.L.8    Zhao, J.H.9
  • 44
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • M. Dubois, K.A. Gilles, J.K. Hamilton, P.A. Rebers, F. Smith, Colorimetric method for determination of sugars and related substances, Anal. Chem. 28 (1956) 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 45
    • 0018394892 scopus 로고
    • A partial modification of the carbazole method of Bitter and Muir for quantitation of hexuronic acids
    • M. Kosakai, Z. Yosizawa, A partial modification of the carbazole method of Bitter and Muir for quantitation of hexuronic acids, Anal. Biochem. 93 (1979) 295-298.
    • (1979) Anal. Biochem. , vol.93 , pp. 295-298
    • Kosakai, M.1    Yosizawa, Z.2
  • 46
    • 0002646228 scopus 로고
    • Infrared spectra of glycosaminoglycans in deuterium oxide and deuterium chloride solution: Quantitative evaluation of uronic acid and acetamidodeoxyhexose moieties
    • B. Casu, G. Scovenna, A.J. Cifonelli, A.S. Perlin, Infrared spectra of glycosaminoglycans in deuterium oxide and deuterium chloride solution: quantitative evaluation of uronic acid and acetamidodeoxyhexose moieties, Carbohydr. Res. 63 (1978) 13-27.
    • (1978) Carbohydr. Res. , vol.63 , pp. 13-27
    • Casu, B.1    Scovenna, G.2    Cifonelli, A.J.3    Perlin, A.S.4
  • 47
    • 0016420420 scopus 로고
    • A conductimetric method for the determination of sulphate and carboxyl groups in heparin and other mucopolysaccharides
    • B. Casu, U. Gennaro, A conductimetric method for the determination of sulphate and carboxyl groups in heparin and other mucopolysaccharides, Carbohydr. Res. 39 (1975) 168-176.
    • (1975) Carbohydr. Res. , vol.39 , pp. 168-176
    • Casu, B.1    Gennaro, U.2
  • 48
    • 0037016675 scopus 로고    scopus 로고
    • Sulfated fucans from the egg jellies of the closely related sea urchins Strongylocentrotus droebachiensis and S. Pallidus ensure species-specific fertilization
    • A.C. Vilela-Silva, M.O. Castro, A.P. Valente, P.A.S. Mourão, Sulfated fucans from the egg jellies of the closely related sea urchins Strongylocentrotus droebachiensis and S. pallidus ensure species-specific fertilization, J. Biol. Chem. 277 (2002) 379-387.
    • (2002) J. Biol. Chem. , vol.277 , pp. 379-387
    • Vilela-Silva, A.C.1    Castro, M.O.2    Valente, A.P.3    Mourão, P.A.S.4
  • 49
    • 84865973883 scopus 로고    scopus 로고
    • Preparation and characterization of O-acylated fucosylated chondroitin sulfate from sea cucumber
    • N. Gao, M.Y. Wu, S. Liu, W. Lian, Z. Li, J. Zhao, Preparation and characterization of O-acylated fucosylated chondroitin sulfate from sea cucumber, Mar. Drugs 10 (2012) 1647-1661.
    • (2012) Mar. Drugs , vol.10 , pp. 1647-1661
    • Gao, N.1    Wu, M.Y.2    Liu, S.3    Lian, W.4    Li, Z.5    Zhao, J.6
  • 50
    • 0024371047 scopus 로고
    • Comparison of two experimental thrombosis models in rats: Effects of four glycosaminoglycans
    • G.M.T. Vogel, D.G. Meuleman, F.G.M. Bourgondiën, P.M. Hobbelen, Comparison of two experimental thrombosis models in rats: effects of four glycosaminoglycans, Thromb. Res. 54 (1989) 399-410.
    • (1989) Thromb. Res. , vol.54 , pp. 399-410
    • Vogel, G.M.T.1    Meuleman, D.G.2    Bourgondiën, F.G.M.3    Hobbelen, P.M.4
  • 51
    • 0346367328 scopus 로고
    • Aggregation of blood platelets by adenosine diphosphate and its reversal
    • G.V.R. Born, Aggregation of blood platelets by adenosine diphosphate and its reversal, Nature 194 (1962) 927-929.
    • (1962) Nature , vol.194 , pp. 927-929
    • Born, G.V.R.1
  • 52
    • 78651139188 scopus 로고
    • The aggregation of blood platelets
    • G.V.R. Born, M.J. Cross, The aggregation of blood platelets, J. Physiol. 168 (1963) 178-195.
    • (1963) J. Physiol. , vol.168 , pp. 178-195
    • Born, G.V.R.1    Cross, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.