Abstract
We constructed a recombinant gene encoding an immunologlobulin (Ig) heavy chain consisting of the variable region from the phosphorylcholine (PC)-specific secreting myeloma MOPC167 and the ε constant region from SJL mice. This gene, cloned into the shuttle vector pSV2gpt, was transfected into J558L myeloma cells, and stable transformants that expressed the ε gene were cloned. The IgE heavy chain in these transformants is associated with the endogenous λ light chain and is secreted as an intact IgE molecule. However, the secreted IgE does not bind to PC conjugated to bovine serum albumin (PC-BSA). The MOPC167 κ chain gene was cloned into the shuttle vector pSV2neo and was transfected into the ε heavy-chain transformant. Stable transformants were cloned that expressed both the ε heavy chain and the κ light chain. IgE secreted from such a transformant was shown to bind to PC-BSA. Both types of secreted recombinant IgE bound to rat basophilic leukemia (RBL) cells, but only the IgE produced by the cell line transformed with the MOPC167 κ gene could be cross-linked with PC-BSA to cause serotonin release.
Original language | English (US) |
---|---|
Pages (from-to) | 324-329 |
Number of pages | 6 |
Journal | Journal of Immunology |
Volume | 138 |
Issue number | 1 |
State | Published - 1987 |
ASJC Scopus subject areas
- Immunology