Microcalorimetric study of the effect of hexa-histidine tag and denaturant on the interaction mechanism between protein and metal-chelating gel

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题名:	Microcalorimetric study of the effect of hexa-histidine tag and denaturant on the interaction mechanism between protein and metal-chelating gel
作者:	Lin,FY;Chen,WY;Chen,HM
贡献者:	化學工程與材料工程研究所
关键词:	ION AFFINITY-CHROMATOGRAPHY;GLUTATHIONE-S-TRANSFERASE;RECOMBINANT PROTEINS;SALT CONCENTRATION;SOFT ACIDS;PH VALUE;HYDROPHOBIC INTERACTION;SCHISTOSOMA-JAPONICUM;STEP PURIFICATION;BASES HSAB
日期:	2001
上传时间:	2010-07-06 16:30:40 (UTC+8)
出版者:	中央大學
摘要:	A recombinant. protein, Schistosoma japonicum glutathione-S-transferase (SjGST), was fused with a C-terminal hexa-histidine tag to obtain SjGST/His. Both proteins were used to probe the interaction mechanisms with the metal ions immobilized on chromatogra
關聯:	JOURNAL OF COLLOID AND INTERFACE SCIENCE
显示于类别:	[化學工程與材料工程研究所] 期刊論文

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