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Anti‐idiotypic antibody identifies the structural similarity between the phosphatidylcholine‐specific monoclonal antibody and phosphatidylcholine‐specific lipid transfer protein
Author(s) -
Nam Kyung Soo,
Umeda Masato,
Igarashi Kouji,
Inoue Keizo
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81201-x
Subject(s) - polyclonal antibodies , idiotopes , monoclonal antibody , phosphatidylcholine , chemistry , phosphatidylserine , microbiology and biotechnology , epitope , antibody , biochemistry , idiotype , phospholipid transfer protein , biology , phospholipid , immunology , membrane
The polyclonal anti‐idiotypic antibody (Anti‐Id) has been raised against a monoclonal antibody (mAb) that specifically binds to phosphatidylcholine (PC). The anti‐Id bound strongly to PC‐specific mAbs, but not to the other mAbs that bind to phosphatidylserine, indicating that the anti‐Id recognizes the cross‐reactive idiotopes expressed on the PC‐specific mAbs. The anti‐Id also showed an extensive cross‐reaction with the PC‐specific lipid transfer protein isolated from bovine liver and inhibited the lipid transfer activity of the protein. These results strongly suggest that the anti‐Id recognizes a common structure shared between PC‐specific mAbs and the PC‐specific lipid transfer protein.