Article
Structural and functional properties of hen egg-white lysozyme deamidated by protein engineering.
Bioscience, biotechnology, and biochemistry - 1 Sept 1992
Kato A, Tanimoto S, Muraki Y, Kobayashi K, Kumagai I
Abstract excerpt
The structural and functional properties of lysozymes genetically deamidated at positions 103 (N103D) and 106 (N106D) were studied by a protein engineering technique. The wild-type and mutant lysozymes were expressed in Saccharomyces cerevisiae and purified from the cultivation medium in two steps by cation-exchange chromatography on CM-Toyopearl. The lytic activity of deamidated lysozymes was almost the same as...
Topics
- Animals
- Base Sequence
- Chickens
- Circular Dichroism
- Deamination
- Egg Proteins
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Muramidase
- Mutation
- Plasmids
