{"title":"红藻紫菜血管紧张素i转换酶抑制剂的纯化与鉴定。","authors":"Suetsuna","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The potent part of the angiotensin I-converting enzyme (ACE) inhibitory activity from Porphyra yezoensis hydrolysate was fractionated by using ion-exchange and gel-filtration techniques. Oral administration of the most potent inhibitory fraction (SP-I fraction, 200 mg/kg) to spontaneously hypertensive rats (SHR) showed a hypotensive effect. Using octadecylsilano column chromatography, the SP-I fraction was further separated into several peptides with potent inhibitory activities. The amino acid sequences of ACE inhibitory peptides derived from Porphyra yezoensis were Ile-Tyr (IC50: 2.69 µM), Met-Lys-Tyr (7.26 µM), Ala-Lys-Tyr-Ser-Tyr (1.52 µM), and Leu-Arg-Tyr (5.06 µM).</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis.\",\"authors\":\"Suetsuna\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The potent part of the angiotensin I-converting enzyme (ACE) inhibitory activity from Porphyra yezoensis hydrolysate was fractionated by using ion-exchange and gel-filtration techniques. Oral administration of the most potent inhibitory fraction (SP-I fraction, 200 mg/kg) to spontaneously hypertensive rats (SHR) showed a hypotensive effect. Using octadecylsilano column chromatography, the SP-I fraction was further separated into several peptides with potent inhibitory activities. The amino acid sequences of ACE inhibitory peptides derived from Porphyra yezoensis were Ile-Tyr (IC50: 2.69 µM), Met-Lys-Tyr (7.26 µM), Ala-Lys-Tyr-Ser-Tyr (1.52 µM), and Leu-Arg-Tyr (5.06 µM).</p>\",\"PeriodicalId\":79672,\"journal\":{\"name\":\"Journal of marine biotechnology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of marine biotechnology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of marine biotechnology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis.
The potent part of the angiotensin I-converting enzyme (ACE) inhibitory activity from Porphyra yezoensis hydrolysate was fractionated by using ion-exchange and gel-filtration techniques. Oral administration of the most potent inhibitory fraction (SP-I fraction, 200 mg/kg) to spontaneously hypertensive rats (SHR) showed a hypotensive effect. Using octadecylsilano column chromatography, the SP-I fraction was further separated into several peptides with potent inhibitory activities. The amino acid sequences of ACE inhibitory peptides derived from Porphyra yezoensis were Ile-Tyr (IC50: 2.69 µM), Met-Lys-Tyr (7.26 µM), Ala-Lys-Tyr-Ser-Tyr (1.52 µM), and Leu-Arg-Tyr (5.06 µM).