- 作者: 李乃元,鄭瑞棠,榎本俊樹,中村一郎
- 作者服務機構: Department Pharmacology, College of Medicine, National Cheng Kung University, Tainan 70101, Taiwan, R.O.C
- 中文摘要: Angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated from the hen ovotransferrin hydrolysate using chymotryptic hydrolysis by two steps of reverse-phase high-performance liquid chromatography. The amino sequence of this novel peptide was identified as Lys-Val-Arg-Glu-Gly-Thr-Thr-Tyr that inhibited ACE activity in vitro in a concentration-dependent manner with an effective concentration (IC50) of 102.8 mM. Also, this inhibition was identified as noncompetitive using the Lineweaver-Burk plot. Moreover, the antihypertensive action of this novel peptide was investigated by an intravenous injection into spontaneously hypertensive rats (SHR). A dose-dependent reduction of systolic blood pressure by this peptide was observed after 40 min of treatment and it decreased the blood pressure markedly at the maximal dose (1 nmol/mL/kg). The maximal blood pressure lowering activity of this peptide was calculated as 163% of captopril (10 pmol/mL/kg) that was used as positive control. In conclusion, the obtained data suggests that Lys-Val-Arg-Glu-Gly-Thr-Thr-Tyr has an ability to inhibit ACE activity and decrease the systolic blood pressure in hypertensive animals.
- 英文摘要: --
- 中文關鍵字: Angiotensin-converting enzyme (ACE) inhibitory peptide; Hen ovotransferrin; Captopril; Spontaneously hypertensive rat.
- 英文關鍵字: --