Article
Mutational analysis of the N-linked glycosylation sites of the human insulin receptor.
The Biochemical journal - 1 May 2000
Elleman T C, Frenkel M J, Hoyne P A, McKern N M, Cosgrove L, Hewish D R, Jachno K M, Bentley J D, Sankovich S E, Ward C W
Abstract excerpt
Site-directed mutagenesis has been used to remove 15 of the 18 potential N-linked glycosylation sites, in 16 combinations, from the human exon 11-minus receptor isoform. The three glycosylation sites not mutated were asparagine residues 25, 397 and 894, which are known to be important in receptor biosynthesis or function. The effects of these mutations on proreceptor processing into alpha and beta subunits,...
Topics
- Animals
- Blotting, Western
- CHO Cells
- Cell Line
- Cricetinae
- Enzyme Activation
- Flow Cytometry
- Glycosylation
- Humans
- Insulin
- Isoelectric Point
- Molecular Weight
- Mutation
- Phosphorylation