Article
Increased proteolytic resistance of ribonuclease A by protein engineering.
Protein engineering - 1 Oct 2001
Markert Y, Köditz J, Mansfeld J, Arnold U, Ulbrich-Hofmann R
Abstract excerpt
Although highly stable toward unfolding, native ribonuclease A is known to be cleaved by unspecific proteases in the flexible loop region near Ala20. With the aim to create a protease-resistant ribonuclease A, Ala20 was substituted for Pro by site-directed mutagenesis. The resulting mutant enzyme was nearly identical to the wild-type enzyme in the near-UV and far-UV circular dichroism spectra, in its activity to...
Topics
- Alanine
- Animals
- Circular Dichroism
- Endopeptidase K
- Enzyme Stability
- Mutagenesis, Site-Directed
- Mutation
- Pancreatic Elastase
- Proline
- Protein Conformation
- Protein Engineering
- Ribonuclease, Pancreatic
- Rosaniline Dyes
- Spectrometry, Fluorescence
- Subtilisins
- Swine
- Thermodynamics