Article
Overproduction and purification of Lon protease from Escherichia coli using a maltose-binding protein fusion system.
Applied microbiology and biotechnology - 1 Nov 1994
Sonezaki S, Kondo A, Oba T, Ishii Y, Kato Y, Nakayama H
Abstract excerpt
Lon protease, which plays a major role in degradation of abnormal proteins in Escherichia coli, was overproduced and efficiently purified using the maltose-binding protein (MBP) fusion vector. The MBP-Lon fusion protein was expressed in a soluble form in E. coli and purified to homogeneity by amylose resin in a single step. Lon protease was split from MBP by cleaving a fusion point between MBP and Lon with factor...
Topics
- 2-Naphthylamine
- ATP-Binding Cassette Transporters
- ATP-Dependent Proteases
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Biotechnology
- Carrier Proteins
- Caseins
- Cloning, Molecular