Six angiotensin I-converting enzyme inhibitory peptides were isolated from a bonito bowels autolysate. Their amino acids were sequenced as Tyr-Arg-Pro-Tyr, Gly-His-Phe, Val-Arg-Pro, Ile-Lys-Pro, Leu-Arg-Pro, and Ile-Arg-Pro. Peptides having corresponding amino acid sequences were synthesized by a solid-phase method and their inhibition of the activity measured. IC50 of these peptides were estimated to be 320, 1100, 2.2, 2.5, 1.0, and 1.8 microM, respectively. The role of carboxyl terminal proline residues on the inhibition is discussed.
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Matsumura et al. (1993) studied this question.