کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10553872 | 967941 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
A direct, extraction-free spectrophotometric assay was developed for determination of angiotensin I-converting enzyme activity (ACE) in the presence of ACE inhibitors using hippuryl-l-histidyl-l-leucine (HHL) as the ACE-specific substrate. This method relies on previously published spectrophotometric determination of hippuric acid (HA) content in the urine, the method of which was based on the specific colorimetric reaction of HA with benzene sulfonyl chloride (BSC) in the presence of quinoline. The proposed ACE inhibition assay was applied to the measurement of the ACE inhibitory activity of Captopril. IC50 value of Captopril corresponded well with literature data. Furthermore, Alcalase hydrolysates of mung bean and rice protein isolates were assessed for ACE inhibitory activity by this method. These two hydrolysates showed high ACE inhibitory activity. This method proposed here was shown to be direct, sensitive, accurate, reproducible, and less expensive without separation of HA from ACE reaction mixture, and can be used for the screening of ACE inhibitory peptides derived from food proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Pharmaceutical and Biomedical Analysis - Volume 37, Issue 2, 23 February 2005, Pages 219-224
Journal: Journal of Pharmaceutical and Biomedical Analysis - Volume 37, Issue 2, 23 February 2005, Pages 219-224
نویسندگان
Guan-Hong Li, Huan Liu, Yong-Hui Shi, Guo-Wei Le,