Article
Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system.
Journal of biochemistry - 1 Nov 1998
Masumoto H, Yoshizawa T, Sorimachi H, Nishino T, Ishiura S, Suzuki K
Abstract excerpt
Recombinant human m-calpain was produced in a soluble form at a level of 20 mg/liter of Sf-9 cell culture by the coexpression of recombinant human m-calpain large (m80K) and small (30K) subunits using a baculovirus expression system. The expressed m-calpain was purified by sequential column chrom...
Topics
- Amino Acid Sequence
- Animals
- Baculoviridae
- Binding Sites
- Calpain
- Chromatography, Gel
- Chromatography, Ion Exchange
- Cloning, Molecular
- Electrophoresis, Polyacrylamide Gel
- Humans
- Molecular Sequence Data
- Mutation
- Rabbits
- Recombinant Proteins