Sulfonation of papain-treated chitosan and its mechanism for anticoagulant activity

Carbohydrate Research

Volumn 344, Issue 10, 2009, Pages 1190-1196

  Suwan, Jiraporn ^a   Zhang, Zhenqing ^d   Li, Boyangzi ^d   Vongchan, Preeyanat ^b   Meepowpan, Puttinan ^c   Zhang, Fuming ^d   Mousa, Shaker A ^h   Mousa, Shaymaa ^h   Premanode, Bhusana ^g   Kongtawelert, Prachya ^a   Linhardt, Robert J ^d,e,f  

^a THAMMASAT UNIVERSITY   (Thailand)

^b Faculty of Associated Medical Sciences   (Thailand)

^c CHIANG MAI UNIVERSITY   (Thailand)

^d Research Rensselaer Polytechnic Institute   (United States)

^e RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^f RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^g IMPERIAL COLLEGE LONDON   (United Kingdom)

^h ALBANY COLLEGE OF PHARMACY AND HEALTH SCIENCES   (United States)

Author keywords

Anticoagulant activity; Chitin; Chitosan polysulfate; Sulfonation

Indexed keywords

ANTICOAGULANT ACTIVITIES; ANTICOAGULANT ACTIVITY; ANTITHROMBIN III; BLOOD CLOTTING; CHLOROSULFONIC ACID; FTIR; HEPARIN COFACTOR II; HETEROGENEOUS CONDITIONS; LOW MOLECULAR WEIGHT; MOLECULAR BINDING; N ,N-DIMETHYLFORMAMIDE; PROTHROMBIN TIME; SULFATED CHITOSAN; THROMBIN TIME;

BINDING SITES; CHITOSAN; DIMETHYLFORMAMIDE; FOURIER TRANSFORM INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYSACCHARIDES; SULFONATION; SURFACE PLASMON RESONANCE; TWO DIMENSIONAL;

CHITIN;

ANTICOAGULANT AGENT; ANTITHROMBIN III; CHITOSAN DERIVATIVE; CHITOSAN POLYSULFATE; HEPARIN COFACTOR II; PAPAIN; UNCLASSIFIED DRUG;

ANTICOAGULATION; ARTICLE; CONTROLLED STUDY; DEPOLYMERIZATION; DRUG MECHANISM; DRUG PROTEIN BINDING; DRUG SYNTHESIS; HUMAN; MOLECULAR WEIGHT; NORMAL HUMAN; PARTIAL THROMBOPLASTIN TIME; PRIORITY JOURNAL; PROTHROMBIN TIME; SULFONATION; THROMBIN TIME; THROMBOELASTOGRAPHY;

ANTICOAGULANTS; ANTITHROMBIN III; CHITOSAN; HEPARIN COFACTOR II; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR WEIGHT; PAPAIN; SULFONIC ACIDS;

EID: 66649109421     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carres.2009.04.016     Document Type: Article

References (31)

1. Robert G.A.F. Chitin Chemistry (1992), McMillan, Houndmills and London
2. Kweon D.K., Song S.B., and Park Y.Y. Biomaterials 24 (2003) 1595-1601
3. Vongchan P., Sajomsang W., Subyen D., and Kongtawelert P. Carbohydr. Res. 337 (2002) 1239-1242
4. Nishimura S.I., Kai H., Shinada K., Yoshida T., Tokura S., Kurita K., Nakashima H., Yamamoto N., and Uryu T. Carbohydr. Res. 306 (1998) 427-433
5. Jayakumar R., Nwe N., Tokura S., and Tamura H. Int. J. Biol. Macromol. 40 (2007) 175-181
6. Jordan J.L., Henderson S., Elson C.M., Zhou J., Kydonieus A., Downie J., and Lee T.D. Urology 70 (2007) 1014-1018
7. Franz G., Pauper D., and Alban S. Proc. Phytochem. Soc. Eur. 44 (2000) 47-58
8. Bjork I., Olson S.T., and Shore J.D. In: Lane D.A., and Lindahl U. (Eds). Chemical and Biological Properties, Clinical Applications (1989), Edward Arnold, London 229-255
9. Lane D.A., Denton J., Flynn A.M., Thunberg L., and Lindahl U. Biochem. J. 218 (1984) 725-732
10. Laurent T.C., Tengblad A., Thunberg L., Hook M., and Lindahl U. Biochem. J. 175 (1978) 691-701
11. Choay J., Petitou M., Lormeau J.C., Sinay P., Casu B., and Gatti G. Biochem. Biophys. Res. Commun. 116 (1983) 492-499
12. Kishimoto T.K., Viswanathan K., Ganguly T., Elankumaran S., Smith S., Pelzer K., Lansing J.C., Sriranganathan N., Zhao G., Galcheva-Gargova Z., Al-Hakim A., Bailey G.S., Fraser B., Roy S., Rogers-Cotrone T., Buhse L., Whary M., Fox J., Nasr M., Dal Pan G.J., Shriver Z., Langer R.S., Venkataraman G., Austen K.F., Woodcock J., and Sasisekharan R. N. Eng. J. Med. 358 (2008) 2457-2467
13. Guerrini M., Beccati D., Shriver Z., Naggi A., Viswanathan K., Bisio A., Capila I., Lansing J.C., Guglieri S., Fraser B., Al-Hakim A., Gunay N.S., Zhang Z., Robinson L., Buhse L., Nasr M., Woodcock J., Langer R., Venkataraman G., Linhardt R.J., Casu B., Torri G., and Sasisekharan R. Nat. Biotechnol. 26 (2008) 669-675
14. Maruyama T., Toida T., Imanari T., Yu G., and Linhardt R.J. Carbohydr. Res. 306 (1998) 35-43
15. Nardella A., Chaubet F., Boisson-Vidal C., Blondin C., Durand P., and Jozefonvicz J. Carbohydr. Res. 289 (1996) 201-208
16. Huang R., Du Y., Yang J., and Fan L. Carbohydr. Res. 338 (2003) 483-489
17. Vikhoreva G., Bannikova G., Stolbushkina P., Panov A., Drozd N., Makarov V., Varlamov V., and Gal'braikh L. Carbohydr. Polym. 62 (2005) 327-332
18. Vishu Kumar A.B., Varadaraj M.C., Lalitha R.G., and Tharanathan R.N. Biochim. Biophys. Acta 1670 (2004) 137-146
19. Gamzazade A., Skyyar A., Nasibov S., Suskov A., and Knirel Yu A. Carbohydr. Polym. 34 (1997) 113-116
20. Kumar A.B., Gowda L.R., and Tharanathan R.N. Eur. J. Biochem. 271 (2004) 713-723
21. Kumar B.A., Varadaraj M.C., and Tharanathan R.N. Biomacromolecules 8 (2007) 566-572
22. Edens R.E., al-Hakim A., Weiler J.M., Rethwisch D.G., Fareed J., and Linhardt R.J. J. Pharm. Sci. 81 (1992) 823-827
23. Matsubara K., Matsuura Y., Bacic A., Liao M., Hori K., and Miyazawa K. Int. J. Biol. Macromol. 28 (2001) 395-399
24. Hirano S., Tanaka Y., Hasegawa M., Tobetto K., and Nishioka A. Carbohydr. Res. 137 (1985) 205-215
25. Iqbal O., and Mousa S.A. In: Mousa S.A. (Ed). Anticoagulants, Antiplatelets and Thrombolytics (2004), Humana, Totowa, New Jersy 9-20
26. Tollefsen D.M. Adv. Exp. Med. Biol. 313 (1992) 167-176
27. Yu H., Munoz E.M., Edens R.E., and Linhardt R.J. Biochim. Biophys. Acta, Gen. Sub. 1726 (2005) 168-176
28. Olson S.T., and Bjork I. In: Lane D.A. (Ed). Advances in Experimental Medicine and Biology Vol. 313 (1992), Plenum, New York 155-165
29. Olson S.T., Srinivasan K.R., Bjork I., and Shore J.D. J. Biol. Chem. 256 (1981) 11073-11079
30. Lindahl U., Backstrom G., Thunberg L., and Leder I.G. Proc. Natl. Acad. Sci. U.S.A. 77 (1980) 6551-6555
31. Mousa S.A., Khurana S., and Forsythe M.S. Arterioscler. Thromb. Vasc. Biol. 20 (2000) 1162-1167