Monoclonal antibodies which differentiate high‐ and low‐affinity binding sites of interleukin‐2

FEBS Letters

Ide, Misao¹  Murai, Yasuo¹  Takemoto, Hiroshi¹ 

[1] Shionogi Research Laboratories, Shionogi & Co., Ltd., 5-12-4 Sagisu Fukushima-ku, Osaka 533, Japan

关键词: Monoclonal antibody;    Interleukin-2;    Interleukin-2 receptor;   

DOI  :  10.1016/0014-5793(88)80983-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Five monoclonal antibodies (L15, L20, L23, L34, and L61) against human recombinant interleukin-2 were tested for their effects on the interleukin-2 bioactivity and binding. Four of these monoclonal antibodies, L15, L20, L34, and L61, which had neutralizing activity, completely blocked interleukin-2 binding to the high-affinity receptor. On the other hand, L23, which had a very weak neutralizing activity, blocked interleukin-2 binding to the low-affinity receptor. These results suggest that there are at least two distinct binding sites on the interleukin-2 molecule; those for the high-affinity receptor and those for the low-affinity receptor. These monoclonal antibodies should be useful tools in the study of the interaction between interleukin-2 and interleukin-2 receptor.

【 授权许可】

Unknown