Characterization of an antihypertensive angiotensin I-converting enzyme inhibitory peptide from the edible mushroom Hypsizygus marmoreus.
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Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension.The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP.Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.
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Affiliation: Department of Biomedicinal Science and Biotechnology, PaiChai University, Daejeon 302-735, Republic of Korea.
ABSTRACT
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Hypertension is one of the very serious diseases and, recently, hypertensive patient longevity has been increased significantly. Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-converting enzyme (ACE) inhibitor in water extracts from the brown-cultivar-fruiting-body of Hypsizygus marmoreus was purified with ultrafiltration, C18 solid phase extraction chromatography and reverse-phase HPLC, and the purified ACE inhibitor with inhibitory activity of IC50 value of 0.19 mg/mL was obtained. The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP. Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat. Related in: MedlinePlus |
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fig5: Lineweaver-Burk plot of ACE activity in the presence of the purified ACE inhibitor (P-2). (▲; Control, ■; 0.1 mg of inhibitor, ×; 0.3 mg of inhibitor). Mentions: The inhibitory pattern of the purified ACE inhibitor P-2 was investigated using a Lineweaver-Burk plot (Figure 5). It was found that the purified ACE inhibitor had a noncompetitive inhibitory pattern, unlike those of Grifola frondosa [7] and Tricholoma giganteum [9], which showed patterns of competitive inhibition. |
View Article: PubMed Central - PubMed
Affiliation: Department of Biomedicinal Science and Biotechnology, PaiChai University, Daejeon 302-735, Republic of Korea.