[1] Gandhi N S, Mancera R L. The structure of glycosaminoglycans and their interactions with proteins[J]. Chem Biol Drug Des, 2008,72(6):455-482.[2] Yamada S, Sugahara K, Ozbek S. Evolution of glycosaminoglycans: Comparative biochemical study[J]. Commun Integr Biol, 2011,4(2):150-158.[3] 张天民, 凌沛学. 糖胺聚糖研究新进展[J]. 食品与药品, 2008,10(5):1-5.[4] Adebowale A O,Cox D S, LIANG Zhongming, et al. Analysis of Glucosamine and Chondroitin Sulfate Content in Marketed Products and the Caco-2 Permeability of Chondroitin Sulfate Raw Materials[J].J Am Nutr Assoc,2000,3:37-44.[5] Kawano T, Suyama T, Nagal J, et al. Low molecular chondroitin sulfate and method for manufacturing the same:US, 3405120[P].1968-10-08.[6] Garron M L, Cygler M. Structural and mechanistic classification of uronic acid-containing polysaccharide lyases[J]. Glycobiology, 2010,20(12):1547-1573.[7] Yamagata T, Saito H, Habuchi O, et al. Purification and properties of bacterial chondroitinases and chondrosulfatases[J]. J Biol Chem, 1968,243(7):1523-1535.[8] Hong S W, Kim B T, Shin H Y, et al. Purification and characterization of novel chondroitin ABC and AC lyases from Bacteroides stercoris HJ-15, a human intestinal anaerobic bacterium[J]. Eur J Biochem, 2002,269(12):2934-2940.[9] Tkalec A L, Fink D, Blain F, et al. Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum[J]. Appl Environ Microbiol, 2000,66(1):29-35.[10] Linhardt R J, Avci F Y, Toida T, et al. CS lyases: structure, activity, and applications in analysis and the treatment of diseases[J]. Adv Pharmacol, 2006,53:187-215.[11] Shibata S, Midura R J, Hascall V C. Structural analysis of the linkage region oligosaccharides and unsaturated disaccharides from chondroitin sulfate using CarboPac PA1[J]. J Biol Chem, 1992,267(10):6548-6555.[12] Hardingham T E, Fosang A J, Hey N J, et al. The sulphation pattern in chondroitin sulphate chains investigated by chondroitinase ABC and ACII digestion and reactivity with monoclonal antibodies[J]. Carbohydr Res, 1994,255:241-254.[13] Brown M D. Method for treating intervertebral disc displacement with enzymes: US, 4696816 [P].1987-09-29.[14] Kato F, Mimatsu K, Iwata H, et al. Comparison of tissue reaction with chondroitinase ABC and chymopapain in rabbits as the basis of clinical application in chemonucleolysis[J]. Clin Orthop Relat Res, 1993(288):294-302.[15] Henke C A, Roongta U, Mickelson D J, et al. CD44-related chondroitin sulfate proteoglycan, a cell surface receptor implicated with tumor cell invasion, mediates endothelial cell migration on fibrinogen and invasion into a fibrin matrix[J]. J Clin Invest, 1996,97(11):2541-2552.[16] Denholm E M, Lin Y Q, Silver P J. Anti-tumor activities of chondroitinase AC and chondroitinase B: inhibition of angiogenesis, proliferation and invasion[J]. Eur J Pharmacol, 2001,416(3):213-221.[17] Pojasek K, Shriver Z, Kiley P, et al. Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum[J]. Biochem Biophys Res Commun, 2001,286(2):343-351.[18] Sorensen H P, Mortensen K K. Advanced genetic strategies for recombinant protein expression in Escherichia coli[J]. J Biotechnol, 2005,115(2):113-128.[19] Hor L I, Shuman H A. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex[J]. J Mol Biol, 1993,233(4):659-670.[20] Srinivasan U, Bell J A. A convenient method for affinity purification of maltose binding protein fusions[J]. J Biotechnol, 1998,62(3):163-167.[21] Eliseev R, Alexandrov A, Gunter T. High-yield expression and purification of p18 form of Bax as an MBP-fusion protein[J]. Protein Expr Purif, 2004,35(2):206-209.[22] Chen Y, Xing X H, Lou K. Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein[J]. BIOCHEMICAL ENGINEERING JOURNAL, 2005,23(2):155-159.[23] Huang W, Boju L, Tkalec L, et al. Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis[J]. Biochemistry, 2001,40(8):2359-2372.[24] Fethiere J, Eggimann B, Cygler M. Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes[J]. J Mol Biol, 1999,288(4):635-647.[25] Chen Y, Xing X H, Ye F C, et al. Production of MBP-HepA fusion protein in recombinant Escherichia coli by optimization of culture medium[J]. BIOCHEMICAL ENGINEERING JOURNAL, 2007,34(2):114-121.[26] Gu K, Linhardt R J, Laliberte M, et al. Purification, characterization and specificity of chondroitin lyases and glycuronidase from Flavobacterium heparinum[J]. Biochem J, 1995,312 ( Pt 2):569-577.[27] Ye F C, Kuang Y, Chen S, et al. Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I[J]. BIOCHEMICAL ENGINEERING JOURNAL, 2009,46(2):193-198.[28] 叶逢春.多功能融合肝素酶的设计及其制备低分子量肝素工艺[D].北京:清华大学,2010.[29] Chen S, Ye F, Chen Y, et al. Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: implications for a comprehensive thermostabilization strategy[J]. Biotechnol Bioeng, 2011,108(8):1841-1851.[30] 叶逢春, 陈银, 邢新会. 重组大肠杆菌生产可溶性MBP融合肝素酶的培养条件优化[J]. 生物加工过程, 2006,4(3):28-32.[31] Chen S, Huang Z, Wu J, et al. Combination of site-directed mutagenesis and calcium ion addition for enhanced production of thermostable MBP-fused heparinase I in recombinant Escherichia coli.[J]. Applied microbiology and biotechnology, 2013,97(7):2907-2916. |