Matsumura N, Fujii M, Takeda Y, Sugita K, Shimizu T
Foods Division, Asahi Chemical Industry Co., Ltd. Shizuoka, Japan.
Biosci Biotechnol Biochem. 1993 May;57(5):695-7. doi: 10.1271/bbb.57.695.
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.
从鲣鱼肠道自溶物中分离出六种血管紧张素I转换酶抑制肽。它们的氨基酸序列分别为Tyr-Arg-Pro-Tyr、Gly-His-Phe、Val-Arg-Pro、Ile-Lys-Pro、Leu-Arg-Pro和Ile-Arg-Pro。通过固相法合成了具有相应氨基酸序列的肽，并测定了它们对该活性的抑制作用。这些肽的半数抑制浓度（IC50）分别估计为320、1100、2.2、2.5、1.0和1.8微摩尔。讨论了羧基末端脯氨酸残基在抑制作用中的作用。
