Article
Formation of a disulfide bond in the immunoglobulin domain of the myelin P0 protein is essential for its adhesion.
Journal of neurochemistry - 1 Jul 1994
Zhang K, Filbin M T
Abstract excerpt
It is widely accepted, although never demonstrated, that the formation of a disulfide bond in the majority of immunoglobulin (Ig)-like domains stabilizes their final conformation and thus is essential to their functioning as adhesion/recognition molecules. The myelin P0 protein, which has been shown directly to behave as a homophilic adhesion molecule, contains a single Ig-like domain, stabilized by a putative...
Topics
- Animals
- Blotting, Western
- CHO Cells
- Cell Adhesion Molecules
- Cricetinae
- Cysteine
- DNA
- Disulfides
- Enzyme-Linked Immunosorbent Assay
- Immunoglobulins
- Mutation
- Myelin P0 Protein
