Article
C1 binding by mouse IgM. The effect of abnormal glycosylation at position 402 resulting from a serine to asparagine exchange at residue 406 of the mu-chain.
The Journal of biological chemistry - 25 Jun 1990
Wright J F, Shulman M J, Isenman D E, Painter R H
Abstract excerpt
We have previously shown that IgM-Asn406, a mutant IgM which has asparagine in place of the serine which is normally found at position 406, also has an abnormally glycosylated mu-chain and is defective in complement-dependent cytolysis. Here we show by analyzing cyanogen bromide fragments from no...
Topics
- Amino Acid Sequence
- Asparagine
- Complement C1
- Glycosylation
- Humans
- Immunoglobulin M
- Immunoglobulin mu-Chains
- Kinetics
- Molecular Sequence Data
- Mutation
- Osmolar Concentration
- Protein Binding
- Serine