Article
C1q binding properties of monomer and polymer forms of mouse IgM mu-chain variants. Pro544Gly and Pro434Ala.
Journal of immunology (Baltimore, Md. : 1950) - 1 Dec 1994
Taylor B, Wright J F, Arya S, Isenman D E, Shulman M J, Painter R H
Abstract excerpt
The effect of replacing proline with alanine at position 434 in the C mu 3 domain (P434A) and with glycine at position 544 in the C mu 4 domain (P544G) of the mu-chain of mouse IgM has been studied. The P434A substitution results in the loss of measurable complement-mediated cytolytic activity (CML) and a decrease in the association rate constant at low ionic strength (mu = 0.06), that results in a diminished Ka...
Topics
- Animals
- Biopolymers
- Cell Line
- Complement Activation
- Complement C1q
- Cytotoxicity, Immunologic
- Hybridomas
- Immunoglobulin M
- Mice
- Mutation
- Protein Binding