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Isolation of an Angiotensin I-Converting Enzyme Inhibitory Protein with Antihypertensive Effect in Spontaneously Hypertensive Rats from the Edible Wild Mushroom Leucopaxillus tricolor

文献类型： 外文期刊

作者： Geng, Xueran 1 ; Tian, Guoting 3 ; Zhang, Weiwei 1 ; Zhao, Yongchang 3 ; Zhao, Liyan 4 ; Ryu, Mansok 1 ; Wang, Hexiang 1 ;

作者机构： 1.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China

2.China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China

3.Yunnan Acad Agr Sci, Inst Biotechnol & Germplasm Resource, Kunming 650223, Peoples R China

4.Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Jiangsu, Peoples R China

5.Chinese Univ Hong Kong, Fac Med, Sch Biomed Sci, Shatin, Hong Kong, Peoples R China

关键词： Leucopaxillus tricolor;ACE inhibitory protein;inhibitory pattern;spontaneously hypertensive rat

期刊名称：MOLECULES （ 影响因子：4.411； 五年影响因子：4.587 ）

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收录情况： SCI

摘要： An 86-kDa homodimeric angiotensin I-converting enzyme (ACE) inhibitory protein designated as LTP was isolated from fruit bodies of the mushroom Leucopaxillus tricolor. The isolation procedure involved ultrafiltration through a membrane with a molecular weight cutoff of 10-kDa, ion exchange chromatography on Q-Sepharose, and finally fast protein liquid chromatography-gel filtration on Superdex 75. LTP exhibited an IC50 value of 1.64 mg.mL(-1) for its ACE inhibitory activity. The unique N-terminal amino acid sequence of LTP was disclosed by Edman degradation to be DGPTMHRQAVADFKQ. In addition, seven internal sequences of LTP were elucidated by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Results of the Lineweaver-Burk plot suggested that LTP competitively inhibited ACE. Both LTP and the water extract of L. tricolor exhibited a clear antihypertensive effect on spontaneously hypertensive rats.

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