Trinder glucose activity test

This article is about the diagnostic test for glucose. For the diagnostic test for salicylates that uses a different reagent by the same name, see Trinder spot test.

The Trinder glucose activity test is a diagnostic test used in medicine to determine the presence of glucose or glucose oxidase. The test employs the Trinder reagent, and is a colour change test resulting from the Trinder reaction.

The Trinder reagent, named after P. Trinder of the Biochemistry Department of the Royal Infirmary in Sunderland (see the article listed in further reading), comprises an aminoantipyrine (such as 4-aminoantipyrine) and phenol (p-hydroxybenzene).[1][2]

The Trinder reaction is the reaction between hydrogen peroxide and the phenol and aminoantipyrine to form a quinone (quinoneimine), catalyzed by the presence of a peroxidase (such as horseradish peroxidase).[1][2][3][4][5] The hydrogen peroxide is itself produced by an initial reaction where the glucose is oxidised in the presence of the glucose oxidase catalyst into H2O2 and gluconic acid.[2][3]

The quinone is red-violet in colour,[3][5] with the intensity of the colour being in proportion to the glucose concentration.[3] The colour is measured at 505 nm,[2] 510 nm,[4] or 540 nm.[3]

Diagnostic kits containing the Trinder reagent are available, including one from Sigma-Aldrich.[2]

The Stanbio Single Reagent Glucose Method is based upon the Trinder technique.[3][6]

References

  1. 1 2 That Tjien Ngo (1988). Nonisotopic immunoassay. Plenum Press. p. 71.
  2. 1 2 3 4 5 F. Yamagishi, T. Stanford, and C. van Ast (2001). "Biosensors From Conductive Polymer Transducers and Sol-Gel Encapsulated Bioindicator Molecules". In Michael Alan Butler, P. Vanýsek, and Noboru Yamazoe. Chemical and biological sensors and analytical methods II: proceedings of the international symposium. The Electrochemical Society. p. 223. ISBN 9781566773515.
  3. 1 2 3 4 5 6 Arvind Kumar, Rajiv Kr. Mishra, & Sudhanshu S. Roy (2004). "Studies on Impact of Industrial Pollution on Biochemical and Histological Changes in a Catfish, Mystus vittatus (Bloch)". In Arvind Kumar. Industrial Pollution & Management. APH Publishing. p. 9. ISBN 9788176487740.
  4. 1 2 Carlos G. Dosoretz and Gary Ward (2006). "Peroxidases". In Ashok Pandey, Colin Webb, Carlos Ricardo Soccol, and Christian Larroche. Enzyme technology. Springer. p. 410. ISBN 9780387292946.
  5. 1 2 J.R. Woodward (1990). "Biochemistry and Applications of Alcohol Oxidase from Methylotrophic Yeasts". In Geoffrey A. Codd, Lubbert Dijkhuizen, and F. Robert Tabita. Autotrophic microbiology and one-carbon metabolism. Kluwer Academic Publishers. p. 219. ISBN 0-7923-0656-2.
  6. ↑ P. Gregorini, K. J. Soder, and R. S. Kensinger (2009). "Effects of rumen fill on short-term ingestive behavior and circulating concentrations of ghrelin, insulin, and glucose of dairy cows foraging vegetative micro-swards". J. Dairy Sci. (American Dairy Science Association) 92 (5): 2095–2105. doi:10.3168/jds.2008-1803. PMID 19389967.

Further reading


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