Article
Inhibitory activity and conformational transition of alpha 1-proteinase inhibitor variants.
European journal of biochemistry - 18 Dec 1991
Schulze A J, Huber R, Degryse E, Speck D, Bischoff R
Abstract excerpt
Several variants of alpha 1-proteinase inhibitor (alpha 1-PI) were investigated by spectroscopic methods and characterized according to their inhibitory activity. Replacement of Thr345 (P14) with Arg in alpha 1-PI containing an Arg residue in position 358 (yielding [Thr345----Arg, Met358----Arg]a...
Topics
- Amino Acid Sequence
- Chromatography, High Pressure Liquid
- Chromosome Deletion
- Circular Dichroism
- Cloning, Molecular
- Escherichia coli
- Genetic Variation
- Humans
- Models, Structural
- Molecular Sequence Data
- Molecular Weight
- Mutagenesis, Site-Directed
- Protein Conformation
- Sequence Homology, Nucleic Acid
- Spectrometry, Fluorescence
- Thrombin
- alpha 1-Antitrypsin
