A fluorescence-based protocol for quantifying angiotensin-converting enzyme activity

Nature Protocols

Volumn 1, Issue 5, 2006, Pages 2423-2427

  Sentandreu, Miguel Ángel ^a   Toldrá, Fidel ^a  

^a INSTITUTO DE AGROQUÍMICA Y TECNOLOGÍA DE ALIMENTOS CSIC   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOBENZOYLGLYCYL 4 NITROPHENYLALANYL PROLINE; 2 AMINOHIPPURIC ACID; 2-AMINOBENZOYLGLYCYL-4-NITROPHENYLALANYL-PROLINE; 2-AMINOHIPPURIC ACID; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; HIPPURIC ACID DERIVATIVE; OLIGOPEPTIDE; UNCLASSIFIED DRUG;

ANIMAL; ARTICLE; FLUOROMETRY; IC 50; METABOLISM; METHODOLOGY; RABBIT;

AMINOHIPPURIC ACIDS; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; FLUOROMETRY; INHIBITORY CONCENTRATION 50; OLIGOPEPTIDES; PEPTIDYL-DIPEPTIDASE A; RABBITS;

EID: 34548819013     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.349     Document Type: Article

References (23)

1. Corvol, P., Eyries, M. & Soubrier, F. Handbook of Proteolytic Enzymes (eds. Barrett, A.J., Rawlings, N.D. & Woessner, J.F.) 332-346 (Elsevier Academic Press, London, 2004).
2. Houston, M.C. The role of vascular biology, nutrition and nutraceuticals in the prevention and treatment of hypertension. JANA S 1, 1-71 (2002).
3. Ruprecht, B. et al. Corrected normal values for serumACE by genotyping the deletion-/insertion-polymorphism of the ACE gene. Pneumologie 55, 326-332 (2001).
4. Shibahara, H. et al. Activity of testis angiotensin converting enzyme (ACE) in ejaculated human spermatozoa. Int. J. Androl. 24, 295-299 (2001).
5. Savary, K. et al. Role of the renin-angiotensin system in primitive erythropoiesis in the chick embryo. Blood 105, 103-110 (2005).
6. Kowa, H. et al. Association of the insertion/deletion polymorphism of the angiotensin I-converting enzyme gene in patients of migraine with aura. Neurosci. Lett. 374, 129-131 (2005).
7. Cushman, D.W. & Cheung, H.S. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 20, 1637-1648 (1971).
8. Arihara, K., Nakashima, Y., Mukai, T., Ishikawa, S. & Itoh, M. Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins. Meat Sci. 57 319-324 (2001).
9. Hernandez-Ledesma, B., Martin-Alvarez, P.J. & Pueyo, E. Assessment of the spectrophotometric method for determination of angiotensin-converting-enzyme activity: Influence of the inhibition type. J. Agric. Food Chem. 51, 4175-4179 (2003).
10. Kim, S., Kim, S. & Song, K.B. Purification of an ACE inhibitory peptide from hydrolysates of duck meat protein. Nutr. Food 8, 66-69 (2003).
11. Sentandreu, M.A. & Toldrá, F. A rapid, simple and sensitive fluorescence method for the assay of angiotensin-I converting enzyme. Food Chem. 97, 546-554 (2006).
12. Carmel, A. & Yaron, A. An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrate of angiotensin-I-converting enzyme and of bacterial dipeptidyl carboxypeptidase. Eur. J. Biochem. 87, 265-273 (1978).
13. Oliveira, E.M., Santos, R.A. & Krieger, J.E. Standardization of a fluorimetric assay for the determination of tissue angiotensin-converting enzyme activity in rats. Braz. J. Med. Biol. Res. 33, 755-764 (2000).
14. Cheviron, N. et al. Coumarin-Ser-Asp-Lys-Pro-OH, a fluorescent substrate for determination of angiotensin-converting enzyme activity via high-performance liquid chromatography. Anal. Biochem. 280 58-64 (2000).
15. Elbl, G. & Wagner, H. A new method for the in vitro screening of inhibitors of angiotensin-converting enzyme (Ace), using the chromophore-labeled and fluorophore-labeled substrate, dansyltriglycine. Planta Med. 57, 137-141 (1991).
16. Cheung, H.S., Wang, F.L., Ondetti, M.A., Sabo, E.F. & Cushman, D.W. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. J. Biol. Chem. 255, 401-407 (1980).
17. Ono, S., Hosokawa, M., Miyashita, K. & Takahashi, K. Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int. J. Food Sci. Technol. 41, 383-386 (2006).
18. Suetsuna, K., Maekawa, K. & Chen, J.R. Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats. J. Nutr. Biochem. 15, 267-272 (2004).
19. Yamamoto, N., Ejiri, M. & Mizuno, S. Biogenic peptides and their potential use. Curr. Pharm. Des. 9, 1345-1355 (2003).
20. Fuglsang, A., Nilsson, D. & Nyborg, N.C. Characterization of new milk-derived inhibitors of angiotensin converting enzyme in vitro and in vivo. J. Enzyme Inhib. Med. Chem. 18, 407-412 (2003).
21. Murray, B.A., Walsh, D.J. & FitzGerald, R.J. Modification of the furanacryloyl-L-phenylalanylglycylglycine assay for determination of angiotensin-I-converting enzyme inhibitory activity. J. Biochem. Bioph. Meth. 59, 127-137 (2004).
22. Sentandreu, M.A. & Toldrá, F. Oligopeptides hydrolysed by muscle dipeptidyl peptidases can generate angiotensin-I converting enzyme inhibitory dipeptides. Eur. Food Res. Technol. (in the press).
23. Sentandreu, M.A. & Toldrá, F. Evaluation of ACE inhibitory activity of dipeptides generated by the action of porcine muscle dipeptidyl peptidases. Food Chem. 101, 1629-1633 (2007).