Abstract:
:Two polypeptides are involved in interleukin 2 binding: a low-affinity receptor of 55 kD (IL2-R alpha) and an intermediate affinity component of 75 kD (IL2-R beta). We describe the cloning by the Polymerase Chain Reaction of the coding region of IL2-R alpha from a human T-cell lymphoma cell line. One clone presented a 72-bp deletion that precisely corresponds to exon 5. The deleted form and the normal IL2-R alpha cDNA were expressed CHO cells. Stable transfected cellular clones were compared for their immunoreactivity to monoclonal antibodies directed against IL2-R alpha and for their ability to bind radiolabeled IL2. The presence or absence of the protein region encoded by exon 5 did not modify the IL2-binding capacity of the receptor.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Mercken L,Moras V,Hemon L,Lionne B,Bousseau A,Dautry-Varsat A,Collins M,Mayaux JFdoi
10.1016/s0006-291x(05)81350-6subject
Has Abstractpub_date
1991-11-14 00:00:00pages
1390-5issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)81350-6journal_volume
180pub_type
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