EFFECT OF ACETYLATION ON CONFORMATION AND BILIRUBIN-BINDING PROPERTIES OF GOAT SERUM-ALBUMIN

Four acetylated derivatives of goat serum albumin with percentage modi fications of 18, 40, 53 and 93% were checked for bilirubin-binding and conformational properties. Acetylation caused marked changes in prote in conformation, as evidenced by double immunodiffusion and proteolyti c digestion results, as well as a decrease in bilirubin binding. An in crease in ionic strength had a dramatic effect-on the bilirubin-bindin g characteristics of modified proteins. The results suggest that the l ysine residues of goat serum albumin modified in this study are not in volved in bilirubin-albumin interaction.