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Co‐refolding denatured‐reduced hen egg white lysozyme with acidic and basic proteins
Author(s) -
Trivedi V.D,
Raman B,
Rao Ch.Mohan,
Ramakrishna T
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01419-1
Subject(s) - lysozyme , chemistry , rnase p , bovine serum albumin , protein aggregation , biochemistry , alcohol dehydrogenase , protein folding , egg white , enzyme , rna , gene
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.