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Biofactors. 1998;7(4):287-98.

Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas.

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  • 1Laboratoire de Biochimie Cellulaire et Moléculaire en Nutrition, EP CHRS 616, Université H. Poincaré, Nancy, France.


The aim of the present work was to study the binding of [125I]-BLGA (beta-lactoglobulin variant A) to the plasma membrane fraction of hybrid cells. This binding increased as a function of time with on-rate and off-rate constant at 4.47 +/- 0.18 x 10(6) M-1 min-1 and 0.17 +/- 0.07 min-1, respectively (n = 3). The saturation study showed a single binding site type corresponding to a Kd at 8.26 +/- 2.98 nM and 14.02 +/- 2.61 x 10(12) sites per mg of the plasma membrane protein (n = 3). Competitive of binding BLGA was observed with BLGA, complexed with retinol and also with RBP (retinol-binding protein). Gel filtration of [125I]-BLGA incubated with Triton X-100 solubilized membrane showed the formation of a ligand-receptor complex. Cross-linking of the tracer to plasma membrane showed a complex with a M(r) at 69 kDa, suggesting a receptor M(r) of 51 kDa, as seen by autoradiography of SDS-PAGE.

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