Article
Immobilization of dihydrofolate reductase by engineered cysteine residue attached to its C-terminal end.
Journal of biochemistry - 1 Sept 1993
Iwakura M, Kokubu T
Abstract excerpt
A cysteine residue with a short amino acid chain spacer was attached to the C-terminal end of mutant dihydrofolate reductase [DHFR(C152E)] by a recombinant DNA technique. By using 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) as a SH reagent, it was determined that the reactivity of the SH group of...
Topics
- Amino Acid Sequence
- Base Sequence
- Cysteine
- Enzymes, Immobilized
- Molecular Sequence Data
- Mutation
- Protein Engineering
- Sepharose
- Sulfhydryl Compounds
- Tetrahydrofolate Dehydrogenase