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在经嗜热菌蛋白酶处理的具有降压活性的弹性蛋白中发现的新型血管紧张素I转换酶抑制肽。

Novel angiotensin I-converting enzyme inhibitory peptides found in a thermolysin-treated elastin with antihypertensive activity.

作者信息

Sato Yuko, Toyoda Tsudoi, Shimizu-Ibuka Akiko, Tamura Tomoko, Kobayashi-Hattori Kazuo, Nakamura Takemichi, Arai Soichi, Mura Kiyoshi

机构信息

Department of Nutrition and Dietetics, Faculty of Family and Consumer Sciences, Kamakura Women's University, Kamakura, Kanagawa, Japan.

出版信息

Biosci Biotechnol Biochem. 2012;76(7):1329-33. doi: 10.1271/bbb.120083. Epub 2012 Jul 7.

Abstract

Angiotensin I-converting enzyme (ACE) inhibitory activity was generated from elastin and collagen by hydrolyzing with thermolysin. The IC50 value of 531.6 µg/mL for ACE inhibition by the elastin hydrolysate was five times less than 2885.1 µg/mL by the collagen hydrolysate. We confirmed the antihypertensive activity of the elastin hydrolysate in vivo by feeding spontaneously hypertensive rats (male) on a diet containing 1% of the elastin hydrolysate for 9 weeks. About 4 week later, the systolic blood pressure of the rats in the elastin hydrolysate group had become significantly lower than that of the control group. We identified novel ACE inhibitory peptides, VGHyp, VVPG and VYPGG, in the elastin hydrolysate by using a protein sequencer and quadrupole linear ion trap (QIT)-LC/MS/MS. VYPGG had the highest IC50 value of 244 µM against ACE and may have potential use as a functional food.

摘要

通过用嗜热菌蛋白酶水解,从弹性蛋白和胶原蛋白中产生了血管紧张素I转换酶(ACE)抑制活性。弹性蛋白水解产物对ACE抑制的IC50值为531.6 µg/mL,比胶原蛋白水解产物的2885.1 µg/mL低五倍。我们通过给自发性高血压大鼠(雄性)喂食含1%弹性蛋白水解产物的饮食9周,在体内证实了弹性蛋白水解产物的降压活性。约4周后,弹性蛋白水解产物组大鼠的收缩压显著低于对照组。我们使用蛋白质测序仪和四极杆线性离子阱(QIT)-LC/MS/MS在弹性蛋白水解产物中鉴定出新型ACE抑制肽VGHyp、VVPG和VYPGG。VYPGG对ACE的IC50值最高,为244 µM,可能具有作为功能性食品的潜在用途。

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