ACE Kit-WST - Amerigo Scientific

- Overview
  - The kit is used for the determination of ACE inhibition activity. ACE works in the Renin-Angiotensin system, which is one of the mechanisms of blood pressure control, to convert Angiotensin I to the vasopressor Angiotensin II. This enzyme also contributes to elevated blood pressure due to its role in breaking down the antihypertensive peptide Bradykinin. In recent years, food and supplements containing ingredients that block ACE have received attention for their use in preventing high blood pressure. The conventional method of measuring ACE inhibition employs the synthetic substrate Hippuryl-His-Leu. Hippuric acid from the synthetic substrate is extracted with ethyl acetate, condensed, redissolved, and then read at an absorbance of 228 nm. This method is cumbersome and measurement is subjected to error due to residual ethyl acetate. ACE inhibition Assay Kit enzymatically detects 3-Hydroxybutyric acid (3HB), which is made from 3-Hydryoxybutyryl-Gly-Gly-Gly (3HB-GGG). Using a 96-well format, it is possible to test multiple samples at one time. In addition, there is no need to use harmful organic solvents, resulting in a safe, simple, and highly reproducible assay.
    
    Please contact us at for specific academic pricing.
- Properties
  - Categories
    
    ACE Activity
    
    Storage
    
    0-5°C
    
    Shipping
    
    ambient temperature
    
    * For research use only
- Applications
  - Application
    
    ACE Inhibition
- Reference
  - 1) L. H. Lam, et al., Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyric acid. Anal Biochem. 2007;364:104-111.
    
    2) L. H. Lam, et al., Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyrate with water-soluble tetrazolium salt. Anal Sci. 2008;24:1057-1060.
    
    3) L. H. Lam, et al., Flow injection analysis of angiotensin I-converting enzyme inhibitory activity with enzymatic reactors. Talanta. 2009;79:1130-1134.
    
    4) Hiromichi Nakamura, et al., Antihypertensive Effects of Continuous Oral Administration of Nattokinase and Its Fragments in Spontaneously Hypertensive Rats. Biol. Pharm. Bull. 2011; 34(11) 1696-1701.
    
    5) C. C. Lau, N. Abdullah and A. S. Shuoib, Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom,Pleurotus cystidiosus O.K. Miller identified by LC-MS/MS, BMC Complement. Altern. Med., 2013, 13, 313.
    
    6) K. Yamaki, Screening Research Methods for α-glucosidase Inhibitors and Angiotensin-converting Enzyme Inhibitors in Fermented Soybean Products and Fermented Milk Products ,JARQ, 2014, 48, 41.
    
    7) C.Lau, N. Abdullah, A. Shuib, and N.Aminudin, Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbachi identified by LC-MS/MS, Food Chemistry, 2014, 148, 396-401.
    
    8) R. Nakabayashi, Z. Yang, T. Nishizawa, T. Mori and K. Saito, Top-down Targeted Metabolomics Reveals a Sulfur-Containing Metabolite with Inhibitory Activity against Angiotensin-Converting Enzyme in Asparagus officinalis, J. Nat. Prod., 2015, 78(5), 1179.
    
    9) M. Alauddin, H. Shirakawa, K. Hiwatashi, A. Shimakage, S. Takahashi, M. Shinbo and M. Komaia, Processed soymilk effectively ameliorates blood pressure elevation in spontaneously hypertensive rats, J. Funct. Foods., 2015, 14, 126.
    
    10) L. Basirico, E. Catalani, P. Morera, S. Cattaneo, M. Stuknyte, U. Bernabucci, I.De Noni, and A. Nardone, Release of angiotensin converting enzyme-inhibitor peptides during in vitro gastrointestinal digestion of Parmigiano Reggiano PDO cheese and their absorption through an in vitro model of intestinal epithelium, Journal of Dairy Science, 2015, 98(11), 7595-7601.
    
    11) T. Hagi, M. Kobayashi, and M. Nomura, Metabolome analysis of milk fermented by gamma-aminobutyric acid-producing Lactococcus lactis, Journal of Dairy Science, 2016, 99(2), 994-1001.