Abstract
Anti-insulin antibody enhanced 125I-insulin binding to liver plasma membranes. Ultrastructural studies revealed that monomeric ferritin-insulin occupied receptors on liver membranes were observed as predominantly single receptors and that increasing concentrations of ferritin-insulin did not alter the distribution patterns. Anti-insulin antibody caused a marked shift in the organizational pattern of insulin receptors from predominantly single receptors to small aggregates of 2–6 receptors.