Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteins

FEBS Letters
V D TrivediT Ramakrishna

Abstract

Refolding of denatured-reduced lysozyme and the effect of co-refolding it with other proteins such as RNase A, bovine serum albumin, histone, myelin basic protein, alcohol dehydrogenase and DNase I on the renaturation yield and the aggregation of lysozyme have been studied. Basic proteins consistently increase the renaturation yield of the basic protein lysozyme (10-20% more than in their absence) with little or no aggregation. On the other hand, co-refolding of lysozyme with acidic proteins leads to aggregation and a significant decrease in renaturation yields. Our results show that hetero-interchain interactions (non-specific interactions) occur when the basic protein lysozyme is refolded together with acidic proteins such as bovine serum albumin, alcohol dehydrogenase or DNase I. Our results also suggest that the net charge on proteins plays a significant role in such non-specific aggregation. These results should prove useful in understanding the hetero-interchain interactions between folding polypeptide chains.

References

Nov 15, 1975·European Journal of Biochemistry·G OrsiniM E Goldberg
Jun 1, 1978·Analytical Biochemistry·D Malamud, J W Drysdale
Jan 1, 1992·Annual Review of Biophysics and Biomolecular Structure·F U HartlW Neupert
May 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·D N BremsC S Tomich
Nov 15, 1986·The Biochemical Journal·F A Marston
Jul 20, 1973·Science·C B Anfinsen
May 1, 1995·Nature Structural Biology·R N Sifers
May 1, 1994·Trends in Biotechnology·R Wetzel
Aug 1, 1994·International Journal of Biological Macromolecules·T K KumarM W Pandit
Aug 20, 1993·Journal of Molecular Biology·T E Gray, A R Fersht
Mar 1, 1994·The Journal of Emergency Medicine·L A Wellford, T M Kelly
Nov 1, 1995·Trends in Biochemical Sciences·P J ThomasP L Pedersen
May 24, 1996·Journal of Molecular Biology·K KatsumataK Kuwajima
Jul 19, 1996·The Journal of Biological Chemistry·B RamanC M Rao
Feb 1, 1997·Current Opinion in Structural Biology·J Martin, F U Hartl

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Citations

Dec 19, 2003·Protein Expression and Purification·Ming LiJan-Christer Janson
May 4, 2005·Protein Expression and Purification·Anton Poliakov, U Helena Danielson
Dec 4, 2003·The International Journal of Biochemistry & Cell Biology·Qiang XieHai-Meng Zhou
Oct 29, 2000·European Journal of Biochemistry·E MartensK Vandenbroeck
Jun 25, 2004·Protein Science : a Publication of the Protein Society·Qin XuGenjun Xu
Dec 31, 2010·Biotechnology and Bioengineering·Guo-Zhen WangYan Sun
Jul 25, 2015·Physical Chemistry Chemical Physics : PCCP·Sergio Romero-RomeroD Alejandro Fernández-Velasco
Dec 17, 2009·Acta Biochimica Et Biophysica Sinica·Ting ZhangXiaoning Wang
Nov 13, 2002·Biochemistry·Thomas D KimChul-Hak Yang

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