Abstract
Goat liver cystatin was subjected to various chemical modifications in order to ascertain the amino acid residues responsible for its structural and functional integrity. Modification of tryptophan by HNBB led to the complete inactivation of the protein. The inactivation was also accompanied by the complete loss of tryptophan fluorescence at 340 nm. The reaction of liver cystatin with HNBB yielded a characteristic decrease in absorbance at 280 nm. Acetylation of the amino groups of liver cystatin was carried out in the presence of acetic anhydride. The acetylated cystatin showed a decrease in fluorescence intensity at 335 nm which could be attributed to the modification of tyrosine residue due to side reaction.