Article
Effects of site-directed removal of N-glycosylation sites in human erythropoietin on its production and biological properties.
The Journal of biological chemistry - 25 Oct 1991
Yamaguchi K, Akai K, Kawanishi G, Ueda M, Masuda S, Sasaki R
Abstract excerpt
Erythropoietin (Epo) has three N-linked sugar chains. Codons for asparagine at N-glycosylation sites in genomic human Epo DNA were replaced with those for glutamine. The wild-type Epo gene and seven mutants that lacked N-glycosylation sites in every possible combination were introduced into baby hamster-kidney cells. To study the role of the N-linked sugars in Epo biosynthesis, Epo protein expressed transiently...
Topics
- Base Sequence
- Blotting, Western
- Cell Line
- Electrophoresis, Polyacrylamide Gel
- Erythropoietin
- Glycosylation
- Humans
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Receptors, Cell Surface