Optical studies on the specific interaction of dipyridamole with alpha 1-acid glycoprotein (orosomucoid).

6533b85efe1ef96bd12bf340

RESEARCH PRODUCT

Optical studies on the specific interaction of dipyridamole with alpha 1-acid glycoprotein (orosomucoid).

Safaa El-gamel The Late Uwe Wollert Walter E Müller

subject

Circular dichroism Chemical Phenomena Stereochemistry Protein Conformation Pharmaceutical Science Orosomucoid In Vitro Techniques Protein structure medicine Humans Pharmacology chemistry.chemical_classification biology Chemistry Physical Circular Dichroism Tryptophan Dipyridamole Orosomucoid Ultraviolet absorbance Dipyridamole Lower affinity chemistry α1 acid glycoprotein biology.protein Tyrosine Spectrophotometry Ultraviolet Glycoprotein Dialysis medicine.drug Protein Binding

description

Abstract The interaction of dipyridamole with α1-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.

year	journal	country	edition	language
1982-03-01	The Journal of pharmacy and pharmacology

10.1111/j.2042-7158.1982.tb04212.x https://pubmed.ncbi.nlm.nih.gov/6121891

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