Linked Life Data

2689571

Source:http://linkedlifedata.com/resource/pubmed/id/2689571

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1990-1-30
pubmed:abstractText
Enzyme immunoassays frequently incorporate the use of horseradish peroxidase as the enzyme label. This enzyme usually catalyses the oxidation of a chromogen which can be quantified after termination of the enzyme reaction. A chromogen widely used for this purpose is 3,3',5,5'-tetramethylbenzidine. The two electron oxidation of tetramethylbenzidine yields a component with an absorbance maximum at 450 nm. If the enzyme reaction is terminated by lowering of the pH (less than 1.0), an additional increase of the absorbance at 450 nm is observed. It is shown that this additional increase is partly due to a 1.4-fold increase in the molar lineic absorbance of oxidized tetramethylbenzidine, caused by the acidic pH, as well as a quantitative shift of the existing equilibrium between tetramethylbenzidine, oxidized tetramethylbenzidine and their charge-transfer complex. The total absorbance increase upon acidification of the reaction mixture depends therefore on the reaction conditions as well as the reaction coordinate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0340-076X
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
791-6
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Some aspects of the chromogen 3,3',5,5'-tetramethylbenzidine as hydrogen donor in a horseradish peroxidase assay.
pubmed:affiliation
Scientific Development Group Organon Int. B.V. Oss, The Netherlands.
pubmed:publicationType
Journal Article