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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1988-10-27
|
| pubmed:abstractText |
Decay curves for tryptophan fluorescence of bovine and human alpha-lactalbumin in different states (metal-free and Ca2+ or Mg2+-loaded states of the native and thermally denatured proteins) have been measured at different wavelengths. The curves are best fitted by a sum of three exponents assigned to emission of individual tryptophan residues. The results suggests that the red shift of the fluorescence spectrum of alpha-lactalbumin caused by release of the bound Ca2+ or thermal denaturation is due to changes in the environment of all emitting tryptophan residues.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0301-4622
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
30
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
105-12
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:3416039-Animals,
pubmed-meshheading:3416039-Cattle,
pubmed-meshheading:3416039-Humans,
pubmed-meshheading:3416039-Kinetics,
pubmed-meshheading:3416039-Lactalbumin,
pubmed-meshheading:3416039-Protein Conformation,
pubmed-meshheading:3416039-Spectrometry, Fluorescence,
pubmed-meshheading:3416039-Tryptophan
|
| pubmed:year |
1988
|
| pubmed:articleTitle |
Environment of tryptophan residues in various conformational states of alpha-lactalbumin studied by time-resolved and steady-state fluorescence spectroscopy.
|
| pubmed:affiliation |
Institute of Biological Physics, U.S.S.R. Academy of Sciences, Pushchino, Moscow.
|
| pubmed:publicationType |
Journal Article
|