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Comparative Study
. 1987 Dec 31;149(3):995-1001.
doi: 10.1016/0006-291x(87)90507-9.

High affinity binding of human interleukin 4 to cell lines

H Cabrillat  1 , J P Galizzi, O Djossou, N Arai, T Yokota, K Arai, J Banchereau
Affiliations
Comparative Study

High affinity binding of human interleukin 4 to cell lines

H Cabrillat et al. Biochem Biophys Res Commun. .

Abstract

Purified human recombinant interleukin 4 (IL-4) was radio iodinated to high specific radioactivity without loss of biological activity. 125I-IL-4 bound specifically to the Burkitt lymphoma Jijoye cells and other cell lines. Jijoye cells showed a high affinity for 125I-IL-4 (Kd approximately equal to 7 10(-11) M) and displayed 1200-1400 specific receptors per cell at 4 degrees C or 37 degrees C. The equilibrium dissociation constant (Kd) corresponds to the IL-4 concentration which induces 50% maximal expression of the low affinity IgE receptor (Fc epsilon RL/CD23) on Jijoye cells. At 4 degrees C the rate constant of association K1 is 1.7 x 10(6) M-1 s-1 and the rate contant of dissociation k -1 is 1.3 x 10(-4) s-1 (t 1/2 = 91 min.) No human recombinant lymphokines other than IL-4 were able to compete for the binding of 125I-IL-4 to its receptor.

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