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Cycloamylose as an efficient artificial chaperone for protein refolding
Author(s) -
Machida Sachiko,
Ogawa Setsuko,
Xiaohua Shi,
Takaha Takeshi,
Fujii Kazutoshi,
Hayashi Kiyoshi
Publication year - 2000
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(00)02258-4
Subject(s) - lysozyme , citrate synthase , chemistry , enzyme , chaperone (clinical) , biochemistry , protein folding , carbonic anhydrase , inclusion bodies , recombinant dna , medicine , pathology , gene
High molecular weight cyclic α‐1,4‐glucan (referred to as cycloamylose) exhibited an artificial chaperone property toward three enzymes in different categories. The inclusion properties of cycloamylose effectively accommodated detergents, which keep the chemically denatured enzymes from aggregation, and promoted proper protein folding. Chemically denatured citrate synthase was refolded and completely recovered it's enzymatic activity after dilution with polyoxyethylenesorbitan buffer followed by cycloamylose treatment. The refolding was completed within 2 h, and the activity of the refolded citrate synthase was quite stable. Cycloamylose also promoted the refolding of denatured carbonic anhydrase B and denatured lysozyme of a reduced form.