Linked Life Data

2069551

Source:http://linkedlifedata.com/resource/pubmed/id/2069551

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-8-14
pubmed:abstractText
The quenching by molecular oxygen of the fluorescence of several probes complexed to apohorseradish peroxidase has been studied by intensity and time-resolved fluorescence methods. The probes utilized include 1-anilino-8-naphthalene sulfonic acid, 4,4'-bis (1-anilino-8-naphthalene sulfonic acid), and 2-p-toluidinylnaphthalene-6-sulfonic acid. These results are contrasted to those obtained using apohorseradish peroxidase complexed with protoporphyrin IX. The resistance of these complexes to denaturation by guanidine hydrochloride was determined. The results demonstrate a dramatic increase in oxygen accessibility to the naphthalene probes compared to protoporphyrin IX, which can be correlated to the increased stability of the protein-protoporphyrin IX complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
178
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
104-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Oxygen diffusion near the heme binding site of horseradish peroxidase.
pubmed:affiliation
Departamento de Química, Facultad de Ciencias, Universidad de Chile, Santiago.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't