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
作者： C Sivakama Sundari , B Raman , D Balasubramanian
DOI: 10.1016/S0014-5793(98)01720-7
关键词:
摘要: … that linear dextrins possess amphiphilic surfaces which can interact with the folding protein, thus preventing self-aggregation and enhancing its renaturation yield. Linear dextrins …
elsevier.com
sci-hub.se 参考文章(28)
J.L. Cleland, C Hedgepeth, D.I. Wang, Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B. Reaction stoichiometry and refolding model. Journal of Biological Chemistry. ,vol. 267, pp. 13327- 13334 ,(1992) , 10.1016/S0021-9258(18)42214-4
Judith Frydman, Jörg Höhfeld, Chaperones get in touch: the Hip-Hop connection. Trends in Biochemical Sciences. ,vol. 22, pp. 87- 92 ,(1997) , 10.1016/S0968-0004(97)01005-0
C A Haase-Pettingell, J King, Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation. Journal of Biological Chemistry. ,vol. 263, pp. 4977- 4983 ,(1988) , 10.1016/S0021-9258(18)68883-0
S Tandon, P Horowitz, Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside. Journal of Biological Chemistry. ,vol. 261, pp. 15615- 15618 ,(1986) , 10.1016/S0021-9258(18)66759-6
Philip L. Whitney, Georg Fölsch, Per Olof Nyman, Bo G. Malmström, Inhibition of human erythrocyte carbonic anhydrase B by chloroacetyl sulfonamides with labeling of the active site. Journal of Biological Chemistry. ,vol. 242, pp. 4206- 4211 ,(1967) , 10.1016/S0021-9258(18)95798-4
J.L. Cleland, T.W. Randolph, Mechanism of polyethylene glycol interaction with the molten globule folding intermediate of bovine carbonic anhydrase B. Journal of Biological Chemistry. ,vol. 267, pp. 3147- 3153 ,(1992) , 10.1016/S0021-9258(19)50707-4
G Zardeneta, P.M. Horowitz, Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation. Journal of Biological Chemistry. ,vol. 267, pp. 5811- 5816 ,(1992) , 10.1016/S0021-9258(18)42625-7
Ronald J. Clarke, John H. Coates, Stephen F. Lincoln, Inclusion Complexes of the Cyclomalto-Oligosaccharides (Cyclodextrins) Advances in Carbohydrate Chemistry and Biochemistry. ,vol. 46, pp. 205- 249 ,(1988) , 10.1016/S0065-2318(08)60167-5
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
Peter Goodenough, Bernhard Fischer, Barry Perry, Ian Sumner, A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies. Protein Engineering. ,vol. 5, pp. 593- 596 ,(1992) , 10.1093/PROTEIN/5.6.593