Article
[Synthesis and characterisation of ATP-dependent forms of Lon-proteinase with modified N-terminal domain from Escherichia coli].
Bioorganicheskaia khimiia - 1 May 1998
Rasulova F S, Dergousova N I, Mel'nikov E E, Ginodman L M, Rotanova T V
Abstract excerpt
The functional domain boundaries of the ATP-dependent Lon proteases were identified by comparative analysis of the amino acid sequences of the enzymes from evolutionarily distant organisms. Modified forms of the Escherichia coli Lon protease with the elongated or substituted N-terminal domain and...
Topics
- ATP-Dependent Proteases
- Adenosine Triphosphate
- Amino Acids
- Cloning, Molecular
- DNA Primers
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression
- Heat-Shock Proteins
- Mutation
- Polymerase Chain Reaction
- Protease La
- Restriction Mapping
- Sequence Deletion
- Serine Endopeptidases