Self-assembling of glutathione S-transferase/calmodulin fusion protein on chemically modified gold surface.
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, 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.
Damrongchai
N
N
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Yun
K
K
Kobatake
E
E
Aizawa
M
M
D002147:Calmodulin / Q000737:chemistry* / Q000235:genetics; D004797:Enzyme-Linked Immunosorbent Assay; D005982:Glutathione Transferase / Q000737:chemistry* / Q000235:genetics; D006046:Gold / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics
D002147:Calmodulin; D011993:Recombinant Fusion Proteins; D006046:Gold; D005982:Glutathione Transferase