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  • Title: Use of circular dichroism to study the interaction of carboxypeptidase A with substrates and inhibitors.
    Author: Arfaoui-Aboulhab L, Jouy M, Fermandjian S, Belhadj O.
    Journal: Arch Inst Pasteur Tunis; 1986; 63(2-3):289-98. PubMed ID: 3778038.
    Abstract:
    The phenylalanyl circular dichroism (CD) bands of peptides were used to assay peptidase activity of carboxypeptidase A (EC.3.4.12.2.). Hippuryl-L-phenylalanine has a sharp, negative CD band at 254 nm whilst L-phenylalanine (the optically active product) has positive CD. Thus the hydrolysis of this substrate as well as the inhibition effect of dipeptides, may be measured from the CD change at 254 nm. The addition of the dipeptide GLy-Tyr to carboxypeptidase A makes the CD spectrum more positive in the region from 270-295 nm. This alteration can result from the tyrosyl and tryptophanyl CD bands of the protein as well as from the tyrosyl CD band of the inhibitor.
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