| Abstract: | Using equilibrium dialysis, protein fluorescence and fluorescent probing as well as chemical modification, the interaction of prostaglandin E2 with human serum albumin was studied. The serum albumin molecule has a highly specific prostaglandin E2-binding site. The binding of prostaglandin causes conformational rearrangements in the protein molecule. The amino group of serum albumin is involved in the interaction with prostaglandin E2. Prolonged exposure of prostaglandin E2 to serum albumin causes partial irreversible binding of prostaglandin molecules to the protein. |
