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

FEBS Letters

Trivedi, V.D¹  Raman, B¹  Ramakrishna, T¹  Rao, Ch.Mohan¹ 

[1]Centre for Cellular and Molecular Biology, Hyderabad 500 007, A.P., India

关键词: Lysozyme;    Refolding;    Acidic protein;    Basic protein;    Inter-chain interaction;   

DOI  :  10.1016/S0014-5793(97)01419-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown