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.
| Trinder glucose activity test | |
|---|---|
| Purpose | determine the presence of glucose |
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 edit
- ^ a b That Tjien Ngo (1988). Nonisotopic immunoassay. Plenum Press. p. 71.
- ^ a b c d e F. Yamagishi; T. Stanford; C. van Ast (2001). "Biosensors From Conductive Polymer Transducers and Sol-Gel Encapsulated Bioindicator Molecules". In Michael Alan Butler; P. Vanýsek; Noboru Yamazoe (eds.). Chemical and biological sensors and analytical methods II: proceedings of the international symposium. Vol. 2001–18. The Electrochemical Society. p. 223. ISBN 9781566773515.
- ^ a b c d e f 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 (ed.). Industrial Pollution & Management. APH Publishing. p. 9. ISBN 9788176487740.
{{cite book}}: CS1 maint: multiple names: authors list (link) - ^ a b Carlos G. Dosoretz; Gary Ward (2006). "Peroxidases". In Ashok Pandey; Colin Webb; Carlos Ricardo Soccol; Christian Larroche (eds.). Enzyme technology. Springer. p. 410. ISBN 9780387292946.
- ^ a b J.R. Woodward (1990). "Biochemistry and Applications of Alcohol Oxidase from Methylotrophic Yeasts". In Geoffrey A. Codd; Lubbert Dijkhuizen; F. Robert Tabita (eds.). Autotrophic microbiology and one-carbon metabolism. Kluwer Academic Publishers. p. 219. ISBN 978-0-7923-0656-6.
- ^ P. Gregorini; K. J. Soder; 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. 92 (5): 2095–2105. doi:10.3168/jds.2008-1803. PMID 19389967.
Further reading edit
- P. Trinder (March 1969). "Determination of blood glucose using an oxidaseperoxidase system with a non-carcinogenic chromogen". J. Clin. Pathol. 22 (2): 158–161. doi:10.1136/jcp.22.2.158. PMC 474026. PMID 5776547.
- Mary Starnes Saunders; William J. French (August 1983). "Enzyme-Linked Immunosorbent Assays for Detection of Xylem-Limited Bacteria: Use of Trinder Reagent". Applied and Environmental Microbiology. 46 (2): 344–347. Bibcode:1983ApEnM..46..344S. doi:10.1128/aem.46.2.344-347.1983. PMC 239384. PMID 16346360.
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