Article
The effects of the site-directed removal of N-glycosylation from cationic peanut peroxidase on its function.
Archives of biochemistry and biophysics - 1 Feb 2001
Lige B, Ma S, van Huystee R B
Abstract excerpt
Peanut peroxidase has been diffracted. The location of its heme and calcium moieties have been shown and their role demonstrated. However, the structure and role of its glycans is only now being elucidated. The role of three N-linked complex glycans on cationic peroxidase (cPrx) of peanut (Arachis hypogaea L cv. Valencia), as expressed by prxPNC1 in transgenic tobacco, was analyzed by site-directed replacement of...
Topics
- Arachis
- Binding Sites
- Blotting, Western
- Catalysis
- Electrophoresis, Polyacrylamide Gel
- Glycosylation
- Guanidine
- Histidine
- Kinetics
- Models, Genetic
- Mutagenesis, Site-Directed
- Mutation
- Peroxidase
- Plants, Genetically Modified
- Plants, Toxic
- Polysaccharides
- Protein Conformation
- Protein Folding