Lactotransferrin receptor of mouse small-intestinal brush border. Binding characteristics of membrane-bound and triton X-100-solubilized forms.

A specific lactotransferrin receptor was identified in the mouse small-intestinal brush-border membrane and the binding features were investigated in homologous and heterologous systems. The receptor was found to be specific for lactotransferrins isolated from milk of various species, but the affinity was higher toward the homologous ligand (Ka = 3.5 x 10(6) M-1 compared with 2.6 x 10(6) M-1 for both human and bovine lactotransferrins). However, the number of binding sites (n) was the same for the three lactotransferrins, namely 0.53 x 10(12)/micrograms of membrane protein. The binding of mouse lactotransferrin to its receptor was found to be pH-dependent, with an optimal binding at pH 5.5, and seemed unlikely to be carbohydrate-mediated. The receptor was demonstrated to be devoid of any affinity for human and mouse serotransferrins or for a 'serotransferrin-like' protein isolated from mouse milk. The receptor was solubilized with 1% Triton X-100 with good yield. The solubilized receptor was found to retain lactotransferrin-binding activity and sensitivity to pH.