Article
Construction of a dimeric form of glutamate dehydrogenase from Clostridium symbiosum by site-directed mutagenesis.
Biochimica et biophysica acta - 17 Oct 1996
Pasquo A, Britton K L, Stillman T J, Rice D W, Cölfen H, Harding S E, Scandurra R, Engel P C
Abstract excerpt
By using site-directed mutagenesis, Phe-187, one of the amino-acid residues involved in hydrophobic interaction between the three identical dimers comprising the hexamer of Clostridium symbiosum glutamate dehydrogenase (GDH), has been replaced by an aspartic acid residue. Over-expression in Esche...
Topics
- Aspartic Acid
- Blotting, Western
- Circular Dichroism
- Cloning, Molecular
- Clostridium
- Dimerization
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Glutamate Dehydrogenase
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Recombinant Proteins
- Ultracentrifugation