An associated molecule, p64, with high-affinity interleukin 2 receptor.
TU11 mAb specific for the human interleukin-2 receptor (IL-2R) beta-chain, p75, co-precipitated two molecules, p64 and p55, with the beta-chain in the lysates of cells bearing the high-affinity IL-2R. The co-precipitation was detected in the presence of IL-2 even in the absence of a chemical cross-linker. H-48 mAb specific for the IL-2R alpha-chain completely pre-absorbed p64 as well as p55 and partially pre-absorbed the beta-chain from the lysates. The co-precipitation was also detected in phytohemagglutinin-stimulated normal peripheral blood lymphocytes, which express the high-affinity IL-2R, but not in the cell line cells bearing only the low-affinity IL-2R. The peptide maps indicate that p64 is a molecule distinct from both the alpha- and beta-chains, and that p55 is identical to the alpha-chain. These findings suggest that p64, along with the alpha- and beta-chains, is a component of the high affinity IL-2R complex, and we have tentatively named it the gamma-chain of IL-2R.
Takeshita
T
T
Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
Asao
H
H
Suzuki
J
J
Sugamura
K
K
D000911:Antibodies, Monoclonal; D006801:Humans; D008970:Molecular Weight; D010449:Peptide Mapping; D011233:Precipitin Tests; D011487:Protein Conformation; D015375:Receptors, Interleukin-2 / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D015375:Receptors, Interleukin-2