Cycloamylose as an efficient artificial chaperone for protein refolding

FEBS Letters

Fujii, Kazutoshi²  Hayashi, Kiyoshi¹  Machida, Sachiko¹  Takaha, Takeshi²  Xiaohua, Shi¹  Ogawa, Setsuko¹ 

[1] National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan;Biochemical Research Laboratory, Ezaki Glico Co. Ltd., Utajima, Nishiyodogawa-ku, Osaka 555-8502, Japan

关键词: Cycloamylose;    Refolding;    Artificial chaperone;    Citrate synthase;    Carbonic anhydrase B;    Lysozyme;   

DOI  :  10.1016/S0014-5793(00)02258-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown