Abstract
β-Glucosidase was purified from lysosomal membranes isolated from rat liver. Binding and uptake of the purified β-glucosidase were mediated via an apparently single binding site on rat peritoneal macrophages. The number of sites and the Kd were 4.20 x 104/cell and 1.00 x 10-7 M, respec-tively. Neither of the processes was inhibited by ligands for mannose/fucose receptors, mannose 6-phosphate receptors, or scavenger receptors, or by other glycoproteins and sugar compounds. A portion of the β-glucosidase taken up into the macrophages was degraded rapidly. These results suggested that liver lysosomal β-glucosidase was endocytosed via a receptor not previously described.
