Self-assembling of glutathione S-transferase/calmodulin fusion protein on chemically modified gold surface

被引:18
作者
Damrongchai, N [1 ]
Yun, K [1 ]
Kobatake, E [1 ]
Aizawa, M [1 ]
机构
[1] TOKYO INST TECHNOL,FAC BIOSCI & BIOTECHNOL,DEPT BIOENGN,MIDORI KU,YOKOHAMA,KANAGAWA 226,JAPAN
关键词
fusion protein; calmodulin; glutathione S-transferase; self assembly; quartz crystal microbalance; molecular assembling;
D O I
10.1016/S0168-1656(97)00063-1
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The fusion protein technique was used to prepare an artificial polyfunctional protein from calmodulin (CaM) and glutathione S-transferase (GST). The fusion protein was designed, expressed, purified, and then assembled to the glutathione self-assembled gold surface. The protein assembly was confirmed through enzyme binding assay and enzyme immunoassay. Specific binding of the fusion protein to glutathione self-assembled on the gold surface was assessed via a quartz crystal microbalance (QCM). The fusion protein was reversibly adsorbed and desorbed by the competitive binding of glutathione present in a solution, thus showing that the binding of the fusion protein was specific and had a highly oriented molecular configuration. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:125 / 133
页数:9
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