title: Self-assembling of glutathione S-transferase/calmodulin fusion protein on chemically modified gold surface.
abstract: 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.
authors.affiliation: Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Damrongchai
authors.forename: K
authors.initials: K
authors.lastname: Yun
authors.forename: E
authors.initials: E
authors.lastname: Kobatake
authors.forename: M
authors.initials: M
authors.lastname: Aizawa
mesh_terms: 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
chemical_list: D002147:Calmodulin; D011993:Recombinant Fusion Proteins; D006046:Gold; D005982:Glutathione Transferase