Linked Life Data

9162152

Source:http://linkedlifedata.com/resource/pubmed/id/9162152

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-5-27
pubmed:abstractText
In the catalyzed reporter deposition technique, horseradish peroxidase catalyzes the activation of conjugated phenolic compounds resulting in the covalent binding of the radicalized intermediates to electron rich moieties in the protein molecules present at the site of reaction. Comparing the biotinyl-, digoxigeninyl-, and fluoresceinyl-derivatives of tyramine and four immunohistochemical formats, we showed that the most sensitive detection system was that using biotinyl-tyramide and an immunohistochemical technique using a biotinylated secondary antibody followed by a streptavidin peroxidase. Amplification without background staining was obtained in most biotin rich tissues with digoxigeninyl-tyramide. With fluoresceinyl-tyramide, clear signal amplification was observed in the fluorescent microscope. Finally, when compared with standard methods, increased sensitivity was obtained with the fluorescent derivative for detection of hybridized sequences in interphase chromosomes.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0242-6498
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
[Amplification of immunologic reactions using catalytic deposition at the reaction sites of tyramine derivatives. A decisive gain in sensitivity in immunohistochemistry and in situ hybridization].
pubmed:affiliation
Laboratoire d'Histopathologie Expérimentale et Moléculaire, Faculté de Médecine BP 184, Vandoeuvre-lès-Nancy.
pubmed:publicationType
Journal Article, English Abstract