SELF-ASSEMBLING OF GLUTATHIONE S-TRANSFERASE CALMODULIN FUSION PROTEIN ON CHEMICALLY-MODIFIED GOLD SURFACE/

Citation
N. Damrongchai et al., SELF-ASSEMBLING OF GLUTATHIONE S-TRANSFERASE CALMODULIN FUSION PROTEIN ON CHEMICALLY-MODIFIED GOLD SURFACE/, Journal of biotechnology, 55(2), 1997, pp. 125-133
Citations number
32
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
01681656
Volume
55
Issue
2
Year of publication
1997
Pages
125 - 133
Database
ISI
SICI code
0168-1656(1997)55:2<125:SOGSCF>2.0.ZU;2-N
Abstract
The fusion protein technique was used to prepare an artificial polyfun ctional protein from calmodulin (CaM) and glutathione S-transferase (G ST). The fusion protein was designed, expressed, purified, and then as sembled to the glutathione self-assembled gold surface. The protein as sembly was confirmed through enzyme binding assay and enzyme immunoass ay. Specific binding of the fusion protein to glutathione self-assembl ed 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.