We report here the primary structure of an immunoglobulin heavy chain synthesized by ICR 16, a variant of the MPC mouse myeloma cell line. The ICR 16 heavy chain is a γ2b-γ2a hybrid, consisting of the C(H)1 domain of γ2b and the hinge, C(H)2, and C(H)3 domains of γ2a subclasses. The genetic mechanism by which ICR 16 occurred may be recombination, based on homologies in both coding and intervening sequences in γ2b and γ2a constant region genes. Although the Fc fragment of ICR 16 is completely γ2a-like and has been shown to bind to γ2a Fc receptors on mouse macrophages, the intact H2L2 molecule is unable to do so. Such an observation underscores the crucial role that conformation may play in the ability of immunoglobulins to carry out biologic functions.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of Immunology|
|State||Published - Jan 1 1982|
ASJC Scopus subject areas
- Immunology and Allergy