PEPTIDE INHIBITORS FOR ANGIOTENSIN-I-CONVERTING ENZYME FROM THERMOLYSIN DIGEST OF DRIED BONITO
PEPTIDE INHIBITORS FOR ANGIOTENSIN-I-CONVERTING ENZYME FROM THERMOLYSIN DIGEST OF DRIED BONITO
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DOI：
10.1271/bbb.56.1541
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发表时间：
1992-10-01
影响因子：
1.6
通讯作者：
YOSHIKAWA, M
中科院分区：
文献类型：
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作者：
YOKOYAMA, K;CHIBA, H;YOSHIKAWA, M
以日本传统的鲣鱼肉为原料，采用不同的蛋白酶对鲣鱼干（Katsuobusi）进行水解，并测定了水解产物对血管紧张素I转化酶（ACE）的抑制活性。3.4.15.1其中，嗜热菌蛋白酶消化物显示出最强的抑制活性。使用HPLC从消化物中分离出八种抑制肽。抑制肽的氨基酸序列为Ile-Lys-Pro-Leu-Asn-Tyr、Ile-Val-Gly-Arg-Pro-Arg-His-Gln-Gly、Ile-Trp-His-His-Thr、Ata-Leu-Pro-His-Ala、Phe-Gln-Pro、Leu-Lys-Pro-Asn-Met、Ile-Tyr和Asp-Tyr-Gly-Leu-Tyr-Pro。通过对多种蛋白质序列的同源性分析，发现其中4种蛋白质与肌动蛋白的一级结构存在同源性。Asp-Met-Ile-Pro-Ala-Gln-Lys是从干鲣鱼的沸水提取物中获得的，该肽存在于肌酸激酶的一级结构中。通过进一步的酶消化或化学合成制备这些肽的片段，并测量它们的ACE抑制活性。其中，Ile-Lys-Pro、Ile-Trp、Leu-Lys-Pro和Leu-Tyr-Pro的抑制活性高于其亲本肽。Ile-Lys-Pro抑制血管紧张素I的高血压活性。
Dried bonito (Katsuobusi), a Japanese traditional seasoning made of bonito muscle was hydrolyzed by various proteases and the inhibitory activity of the hydrolyzates for angiotensin I-converting enzyme (ACE) [EC 3.4.15.1] was measured. Among the digests, thermolysin digest showed the most potent inhibitory activity. Eight inhibitory peptides were isolated from the digest using HPLC. The amino acid sequences of inhibitory peptides were Ile-Lys-Pro-Leu-Asn-Tyr, Ile-Val-Gly-Arg-Pro-Arg-His-Gln-Gly, Ile-Trp-His-His-Thr, Ata-Leu-Pro-His-Ala, Phe-Gln-Pro, Leu-Lys-Pro-Asn-Met, Ile-Tyr, and Asp-Tyr-Gly-Leu-Tyr-Pro. By searching for the sequence homology in many proteins, four of them were found in the primary structure of actin. Asp-Met-Ile-Pro-Ala-Gln-Lys was obtained from the boiling water extract of dried bonito and this peptide was found in the primary structure of creatine kinase. Fragments of these peptides were prepared by further enzymatic digestion or chemical synthesis and their ACE-inhibitory activities were measured. Among them, Ile-Lys-Pro, Ile-Trp, Leu-Lys-Pro, and Leu-Tyr-Pro had higher inhibitory activity than their parental peptides. Ile-Lys-Pro suppressed the hypertensive activity of angiotensin I.