Enzyme-responsive artificial chaperone system with amphiphilic amylose primer
作者： Nobuyuki Morimoto , Naruhito Ogino , Tadashi Narita , Kazunari Akiyoshi
DOI: 10.1016/J.JBIOTEC.2009.01.013
关键词:
摘要: An enzyme-responsive artificial chaperone system which employs an amphiphilic amylose primer (dodecyl maltopentaose, C12-MP) as a surfactant and phosphorylase b was designed to enable protein refolding. Effective refolding of carbonic anhydrase B after both heat denaturation (70 degrees C for 10min) guanidine hydrochloride (6M) observed by controlled association between the molecules C12-MP micelle through enzymatic reaction.
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sci-hub.se 参考文章(26)
Y. Pocker, J. T. Stone, The catalytic versatility of erythrocyte carbonic anhydrase. 3. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry. ,vol. 6, pp. 668- 678 ,(1967) , 10.1021/BI00855A005
C Sivakama Sundari, B Raman, D Balasubramanian, Artificial chaperoning of insulin, human carbonic anhydrase and hen egg lysozyme using linear dextrin chains - a sweet route to the native state of globular proteins FEBS Letters. ,vol. 443, pp. 215- 219 ,(1999) , 10.1016/S0014-5793(98)01720-7
A. Elisabeth Eriksson, T. Alwyn Jones, Anders Liljas, Refined structure of human carbonic anhydrase II at 2.0 A resolution. Proteins. ,vol. 4, pp. 274- 282 ,(1988) , 10.1002/PROT.340040406
Cyrus H. Fiske, Yellapragada Subbarow, THE COLORIMETRIC DETERMINATION OF PHOSPHORUS Journal of Biological Chemistry. ,vol. 66, pp. 375- 400 ,(1925) , 10.1016/S0021-9258(18)84756-1
Y. Pocker, J. T. Stone, The catalytic versatility of erythrocyte carbonic anhydrase. VI. Kinetic studies of noncompetitive inhibition of enzyme-catalyzed hydrolysis of p-nitrophenyl acetate Biochemistry. ,vol. 7, pp. 2936- 2945 ,(1968) , 10.1021/BI00848A034
P. M. Horowitz, Kinetic Control of Protein Folding by Detergent Micelles, Liposomes, and Chaperonins American Chemical Society. pp. 156- 163 ,(1993) , 10.1021/BK-1993-0526.CH012
W. J. Whelan, J. M. Bailey, The action pattern of potato phosphorylase Biochemical Journal. ,vol. 58, pp. 560- 569 ,(1954) , 10.1042/BJ0580560
David Rozema, Samuel H. Gellman, Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry. ,vol. 35, pp. 15760- 15771 ,(1996) , 10.1021/BI961638J
Nobuyuki Morimoto, Naruhito Ogino, Tadashi Narita, Shinichi Kitamura, Kazunari Akiyoshi, Enzyme-responsive molecular assembly system with amylose-primer surfactants Journal of the American Chemical Society. ,vol. 129, pp. 458- 459 ,(2007) , 10.1021/JA065966A
Huub Schellekens, Bioequivalence and the immunogenicity of biopharmaceuticals Nature Reviews Drug Discovery. ,vol. 1, pp. 457- 462 ,(2002) , 10.1038/NRD818