Linked Life Data

7448190

Source:http://linkedlifedata.com/resource/pubmed/id/7448190

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-3-27
pubmed:abstractText
The active site carboxymethylated glyceraldehyde-3-phosphate dehydrogenase from B. stearothermophilus when irradiated with ultraviolet light in the presence of NAD gives rise to a fluorescent derivative closely similar to that obtained from the muscle enzyme in fluorescence properties. A radiationless energy transfer also occurs between the tryptophan residues of the enzyme protein and the new fluorophore, as for the muscle enzyme. Quantitative determinations of the quantum yields and calculations according to the Förster equation five a distance of 26.36 A between the tryptophan residues and the new fluorophore. In contrast to the muscle enzyme, the irradiated thermophilic enzyme contains four fluorescent NAD derivatives per enzyme tetramer as shown by phosphorus analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
613
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
249-55
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Formation and energy transfer of a fluorescent derivative of B. stearothermophilus glyceraldehyde-3-phosphate dehydrogenase.
pubmed:publicationType
Journal Article