Co-solvent mediated thermal stabilization of chondroitinase ABC I form Proteus vulgaris

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• 作者：Mahdieh Nazari-Robati^a ; Khosro Khajeh^b ; Mahdi Aminian^a ; Mehrnoosh Fathi-Roudsari^c ; Abolfazl Golestani^a ; ^{golsetan@tums.ac.ir}
• 关键词：cABC I ; chondroitinase ABC I ; rcABC I ; recombinant chondroitinase ABC I ; C6S ; chondroitin-6-sulfate ; C4S ; chondroitin-4-sulfate ; DS ; dermatan sulfate ; GAGs ; glycosaminoglycans ; SCI ; spinal cord injury ; CD ; circular dichroism
• 刊名：International Journal of Biological Macromolecules
• 出版年：2012
• 期刊代码：62_01418130
• 类别：abs
• 出版时间：1 April, 2012
• 卷：50
• 期：3
• 页码：487-492
• 文件大小：600 K

摘要

Chondroitinase ABC I (cABC I) from Proteus vulgaris cleaves glycosaminoglycan chains which are responsible for most of the inhibition of axon regrowth in spinal cord injury. The clinical utilization of this enzyme is mainly limited by its thermal instability. This study has been undertaken to determine the effects of glycerol, sorbitol and trehalose on cABC I activity and thermal stability. The results indicated that the enzyme catalytic activity and intrinsic fluorescence intensity increased in the presence of these cosolvents whereas no considerable conformational changes observed in far-UV CD spectra. Thermal CD experiment revealed an increase in T_m of cABC I in the presence of cosolvents which was significant for trehalose. Our results support the idea that cABC I has stabilized in the presence of glycerol, sorbitol and trehalose. Therefore, the use of these cosolvents seems to be promising for improvement in shelf-life and clinical applications of this drug enzyme.