[Decreased binding by isolated rat hepatocytes of asialo-haptoglobin after combination with hemoglobin].

The desialilation of 125I-labelled haptoglobin unmasks non-reducing galactose which has become terminal and permits its recognition and binding by isolated hepatocytes. However, the prior formation of an asialohaptoglobin-haemoglobin complex diminishes this property considerably. The explanation suggested is that there could either be a structural rearrangement of the complexed asialo-haptoglobin or steiric hindrance due to a masking of the galactose by the haemoglobin.