Demonstration of Specific Plasma Protein Binding Sites For Somatomedin

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Abstract
Native somatomedin (SM) has an apparent mol wt of at least 60,000 daltons, while all the purified SM peptides have mol wt 5–8,000 daltons. We have studied the behavior of somatomedin in plasma during gel filtration at pH 8.1 and pH 2.8, and by the recombination of fractions. Using porcine bioassay for SM, displacement of 125I-insulin by SM, and binding of 125I-SM to plasma proteins, we can demonstrate that the disparity in apparent mol wt of SM is due to reversible binding o t plasma proteins which are themselves biologically inactive. This binding site is specific for the SM peptides, saturable, and has high affinity and relatively low capacity.