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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1985-9-3
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pubmed:abstractText |
The binding of calcium to whiting (one tryptophan residue) and pike (one tyrosine residue) parvalbumins has been studied by means of kinetic and steady-state fluorescence techniques. The decay curves of the tryptophan and tyrosine fluorescence of the parvalbumins are best fitted by a sum of two exponents for any metal state of the proteins. The data can be interpreted as a nonexponential decay of the fluorescence of a single-type chromophore or in terms of equilibria between compact and relaxed conformers of the parvalbumins in each metal state. Fluorescence quenching by I-ions and effects of H2O/D2O substitution confirm the second interpretation. The constants of the equilibria have been evaluated.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
240
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
781-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3927843-Animals,
pubmed-meshheading:3927843-Calcium,
pubmed-meshheading:3927843-Egtazic Acid,
pubmed-meshheading:3927843-Fishes,
pubmed-meshheading:3927843-Iodine,
pubmed-meshheading:3927843-Isoelectric Point,
pubmed-meshheading:3927843-Kinetics,
pubmed-meshheading:3927843-Mathematics,
pubmed-meshheading:3927843-Muscle Proteins,
pubmed-meshheading:3927843-Parvalbumins,
pubmed-meshheading:3927843-Spectrometry, Fluorescence
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pubmed:year |
1985
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pubmed:articleTitle |
Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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