Prostaglandin F2 alpha binding to bovine ocular and synthetic melanins in vitro.

The binding of 3H-prostaglandin F2 alpha to bovine iris and synthetic melanin was studied in vitro using a ligand binding assay. Prostaglandin F2 alpha was reversibly bound to both types of melanin. The binding was saturable and the Scatchard analysis revealed the existence of at least two binding sites with the corresponding K(D) values of 3.71 nM and 1.99 microM for natural and 4.99 nM and 0.19 microM for synthetic melanin, respectively. The high affinity Bmax values were 3.4 nM/g for natural and 2.5 nM/g for synthetic melanin. The dissociation of prostaglandin F2 alpha from melanin after dilution of the complex was rapid and uniform.