PROTEIN-BINDING OF ASCORBIC-ACID .2. INTERACTION WITH ACETYLSALICYLIC-ACID

  • 1 January 1980
    • journal article
    • research article
    • Vol. 50  (4) , 387-392
Abstract
The effect of aspirin (ASP) on the binding of ascorbic acid (AA) to bovine serum albumin (BSA) was studied using dynamic dialysis. Scatchard plots were constructed which confirmed that binding with AA occurred in the presence of BSA. When ASP was present, greater curvature of the plot was demonstrated indicating that less binding of AA to BSA was taking place. The limiting slopes of the plots showed that ASP displaces both primary and secondary sites previously occupied by AA and that the strengths of both primary and secondary sites increased due to interaction with ASP. Primary sites for binding of AA to BSA consist of 2 or more types of similar binding strengths, and that secondary binding may involve binding on 2 or more sites. The pathophysiological implications are discussed.