Liquid Chromatographic Assay of Peptides Activity with Inhibiting Angiotensin Converting Enzyme
Liquid Chromatographic Assay of Peptides Activity with Inhibiting Angiotensin Converting Enzyme
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发表时间:
2010-11
期刊:
影响因子:
8.8
通讯作者:
Yu Zhi-peng Zhao Wen-zhu Lu Jing Chen Feng Liu Jing-bo-Yu-Zhi-peng-Zhao-Wen-zhu-Lu-Jing-Chen-Feng-Liu-1844064582;Lin Song-yi
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作者:
Yu Zhi-peng Zhao Wen-zhu Lu Jing Chen Feng Liu Jing-bo-Yu-Zhi-peng-Zhao-Wen-zhu-Lu-Jing-Chen-Feng-Liu-1844064582;Lin Song-yi
A rapid, simple and interference-free method was developed to evaluate the inhibitory activity of hydro- lyzed peptides from egg white protein against the angiotensin-converting enzyme. The total reaction volume was 60 μL, saving the cost. The assay was based on a HPLC separation and quantification of the synthetic substrate hip- puryl-L-histidyl-L-leucine and its hydrolyzed product―hippuric acid; the separation was performed on a C18 column eluted by a mobile phase of acetonitrile/water(0.5% TFA) at a volume ratio of 25:75. At a signal to noise ratio(S/N) of 10, the detective limit of the quantitation of hippuric acid was (0.4600±0.0097) μmol/L. The standard curve shows a linear response with a slope of 49488 and a correlation coefficient of 0.9995. The assay was adequate for the study of ACE inhibition by Captopril and peptides derived from food protein, and showed a very good correlation with the previous methods. Keywords Angiotensin converting enzyme; HPLC; Egg white protein; Peptide Article ID 1005-9040(2010)-05-712-05