EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Rapid and simple colorimetric assay for screening angiotensin I-converting enzyme inhibitors


Pharmaceutical Biology 50(10): 1303-1309
Rapid and simple colorimetric assay for screening angiotensin I-converting enzyme inhibitors
Angiotensin-converting enzyme (ACE) is one of the main regulators of blood pressure through its action on the renin-angiotensin system. ACE inhibitory peptides from natural materials inhibit ACE activity and have considerable importance as antihypertensive agents. A new chromogenic reaction method for determining hippuric acid (HA) and angiotensin I-converting enzyme (ACE) inhibitor activity was developed. This method is based on the reaction of HA with p-dimethylaminobenzaldehyde in the presence of quinoline, acetate, and acetic anhydride. The red-orange formation product in the reaction has a stable absorbance in the visible region and it was determined at 478 nm. The assay conditions were optimized and by using an ACE concentration of 12 mU/mL in enzymatic reaction, the method was applied to monitor the IC(50) values (the concentration of inhibitor required to inhibit 50% of the ACE activity) for captopril and Saurida elongata (Synodontidae) muscle protein hydrolyzate. With the proposed method, IC(50) values for captopril and Saurida elongata muscle protein hydrolyzate were determined as 0.0123 µM and 0.1648 mg/mL, respectively. Those results correspond to the IC(50) values of 0.0109 µM and 0.1820 mg/mL obtained by high-performance liquid chromatography (HPLC) method. The proposed method is rapid, accurate, reproducible and convenient, and suitable for screening ACE inhibitor peptides from food materials while it does not require HA extraction from the components of the ACE activity assay reaction.

(PDF same-day service: $19.90)

Accession: 055361995

PMID: 22873831

DOI: 10.3109/13880209.2012.674534



Related references

Colorimetric, high-throughput assay for screening Angiotensin I-converting enzyme inhibitors. Analytical Chemistry 81(22): 9388-9394, 2010

Validation of a colorimetric assay for the in vitro screening of inhibitors of angiotensin-converting enzyme (ACE) from plant extracts. Phytomedicine 12(6-7): 424-432, 2005

Evaluation of a simple colorimetric assay for serum angiotensin-converting enzyme: comparison with a new ion-pair liquid chromatography-assisted assay. Annals of Clinical Biochemistry 19: 227-232, 1982

Evaluation of a test kit for the rapid and simple colorimetric measurement of angiotensin i converting enzyme ec 3.4.15.1 in serum. Journal of Clinical Chemistry and Clinical Biochemistry 21(12): 845-850, 1983

Evaluation of a test kit for the rapid and simple colorimetric measurement of angiotensin I-converting enzyme in serum. Journal of Clinical Chemistry and Clinical Biochemistry. Zeitschrift für Klinische Chemie und Klinische Biochemie 21(12): 845-849, 1983

A rapid and simple spectrophotometric assay of angiotensin converting enzyme. Analytical Biochemistry 84(2): 361-369, 1978

A rapid, simple and sensitive fluorescence method for the assay of angiotensin-I converting enzyme. Food chemistry 97(3): 546-554, 2006

Sensitive colorimetric assay for angiotensin converting enzyme ec 3.4.15.1 in serum. Clinical Chemistry 29(7): 1399-1403, 1983

Sensitive colorimetric assay for angiotensin converting enzyme in serum. Clinical Chemistry 29(7): 1399-1403, 1983

An improved colorimetric assay of angiotensin-converting enzyme in serum. Clinica Chimica Acta; International Journal of Clinical Chemistry 144(1): 71-75, 1984