Transport of metanil yellow in the rat plasma and interaction of its metabolite,p‐aminodiphenylamine with serum proteins

Binding affinity of metanil yellow and its breakdown product p‐aminodiphenylamine to serum proteins has been studied employing chromatographic separation on Sephadex G‐200 and by paper and polyacrylamide gel electrophoresis. Metanil yellow has more affinity towards albumin than to globulins. The complexing is presumably through electrostatic forces. p‐Aminodiphenylamine on the other hand, preferably binds to globulin fractions of serum protein. However, a stable binding with BSA alone was also observed. The binding was quite stable and was accompanied by a shift in absorbance from 430 nm to 500 nm. Aspartic acid moiety of protein was found to be one of the units involved in the binding of p‐ADPA to proteins.