PROTEIN-BINDING OF ASCORBIC-ACID .1. BINDING TO BOVINE SERUM-ALBUMIN

  • 1 January 1980
    • journal article
    • research article
    • Vol. 50  (4) , 380-386
Abstract
A modified method is described for investigating the binding of ascorbic acid (AA) to bovine serum albumin (BSA) by the use of dynamic dialysis. Reversible complex formation occurs between AA and BSA. Non-Linear least-squares curve fitting procedures were used to construct a Scatchard plot. The values of the limiting slopes demonstrated 2 classes of independent binding sites which have different intrinsic binding constants. The binding strengths of the primary sites were .apprx. 300 times greater than those of the secondary sites, but the secondary sites were about 42 times more numerous. The pathophysiological implications are discussed. The concentration of AA in the leukocytes provides an index of the nutritional status of AA in the body. A reliable estimate of the tissue status and metabolic turnover of AA in normal [humans] is obtained when the plasma AA levels are assessed in relation to leukocyte AA concentrations.

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