The pH titration of nine amino acids (glycine, proline, valine, serine
, glutamine, tryptophan, arginine, histidine and aspartic acid) in pre
sence of urea in the concentration range 1-8 mole dm-3 has been perfor
med. The results support suppression of the first dissociation constan
t (K1) of the amino acids and acceptance of H+ ions by the amide formi
ng uronium ion (UH+). The second dissociation constant (K2) of the ami
no acids is affected relatively weakly by urea. Quantitative evaluatio
n of different species existing in solution and the degree of dissocia
tion of the acids as well as the degree of binding of H+ ion to the am
ide have been made. It has been found that the polarity of the aqueous
-urea medium does not straight forwardly correlate with the altered pK
1 of the amino acids. Urea can also affect the pH-titration behaviour
of gelatin with an increase of the intrinsic pK of the acidic groups o
f the protein by 0.45 unit.