Characterization of lipophorin receptor in locust flight muscles

Abstract

The binding of radiolabelled lipophorin to crude preparations of plasma membranes of locust flight muscles was saturable, specific and displaceable by unlabelled ligand. Specific binding increased rapidly during the first 30 s and reached equilibrium within 4 min at 0°C. The bound 14C-labelled lipophorin dissociated from the muscle cell membrane within 30 s of adding excess unlabelled lipophorin. The specific binding of lipophorin serves to transfer diacylglycerol into flight muscle cells but internalization and degradation of the complete lipophorin complex does not occur.