Article
Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins.
The Journal of biological chemistry - 15 Jan 1990
Rubin H, Wang Z M, Nickbarg E B, McLarney S, Naidoo N, Schoenberger O L, Johnson J L, Cooperman B S
Abstract excerpt
Human alpha 1-antichymotrypsin has been cloned, sequenced and expressed in Escherichia coli and recombinant protein as well as point-specific mutants have been purified and characterized. The corrected gene-deduced amino acid sequence has 45% overall identity with alpha 1-protease inhibitor, whic...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Blotting, Western
- Cloning, Molecular
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Gene Expression
- Genes, Bacterial
- Humans
- Kinetics
- Molecular Sequence Data
- Mutation
- Recombinant Proteins
- Swine
- alpha 1-Antichymotrypsin