Real-Time Biospecific Interaction Analysis of Immobilized Interleukin-2 Receptor β-Chain Peptides with Polyclonal Antibodies1

Author(s):  
K. Schmitt ◽  
U. Schwuléra ◽  
I. Amiri ◽  
U. Roder ◽  
Å. Edström ◽  
...  
2005 ◽  
Vol 329 (3) ◽  
pp. 1094-1101 ◽  
Author(s):  
Sang-Kyu Ye ◽  
Tack Joong Kim ◽  
Sung Sik Won ◽  
Taek Joon Yoon ◽  
Tae Kyu Park ◽  
...  

1990 ◽  
Vol 81 (9) ◽  
pp. 902-908 ◽  
Author(s):  
Taiichi Kodaka ◽  
Takashi Uchiyama ◽  
Takayuki Ishikawa ◽  
Masanori Kamio ◽  
Rie Onishi ◽  
...  

Genomics ◽  
1992 ◽  
Vol 12 (1) ◽  
pp. 179-180 ◽  
Author(s):  
Hugh D. Campbell ◽  
Graham C. Webb ◽  
Takeshi Kono ◽  
Tadatsugu Taniguchi ◽  
Judith H. Ford ◽  
...  

1994 ◽  
Vol 24 (9) ◽  
pp. 1951-1955 ◽  
Author(s):  
Agnès Hémar ◽  
Michéle Lieb ◽  
Agathe Subtil ◽  
James P. Disanto ◽  
Alice Dautry-Varsat

1994 ◽  
Vol 59 (4) ◽  
pp. 943-950
Author(s):  
Eugenia Drakopoulou ◽  
Georgia Sotiropoulou ◽  
Vassilis Tsilivakos ◽  
Vassilis Georgoulias ◽  
Paul Cordopatis

The interleukin-2 receptor β-chain (IL-2Rβ) is responsible for the IL-2 internalization and signal transduction. To identify domains from the IL-2Rβ extracellular region which are involved in ligand receptor interactions, eight peptides of 8 to 25 amino acids corresponding to IL-2Rβ sequence 30-54 were synthesized. Their biological effect was tested with [125I]IL-2 equilibrium binding to PHA-blasts. Preincubation of [125I]IL-2 with peptides IL-2Rβ (35-54) and (30-42) affects IL-2 binding to both high and intermediate affinity receptors by revealing a greater number of active sites with lower affinity.


Sign in / Sign up

Export Citation Format

Share Document