Optical studies on the specific interaction of dipyridamole with alpha 1-acid glycoprotein (orosomucoid).
The interaction of dipyridamole with alpha 1-acid glycoprotein was investigated by circular dichroism and ultraviolet absorbance measurements as well as by equilibrium dialysis experiments. Dipyridamole is bound to the protein via one site of extremely high affinity and by at least one site of considerably lower affinity. Only the association of dipyridamole with the high affinity site produces typical extrinsic Cotton effects. As a result of experimental observations it is concluded that the high affinity site is located in a hydrophobic protein structure of the glycoprotein.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002942:Circular Dichroism / Q000379:methods; D003956:Dialysis; D004176:Dipyridamole / Q000097:blood*; D006801:Humans; D066298:In Vitro Techniques; D009961:Orosomucoid / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D014364:Tryptophan; D014443:Tyrosine
D009961:Orosomucoid; D014443:Tyrosine; D004176:Dipyridamole; D014364:Tryptophan