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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 |
1984-2-14
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pubmed:abstractText |
The binding of Na+ and K+ to whiting parvalbumin (pI 4.4) and pike parvalbumins (pI 4.2 and 5.0) results in a shift of the tryptophan fluorescence spectrum towards shorter wavelengths by 2-4 nm for the whiting protein and in a rise of the tyrosine and phenylalanine fluorescence quantum yield for the pike proteins. The effective binding constants of Na+ and K+ to parvalbumins are within the range of 10 M-1 to 100 M-1. Physiological concentrations of Na+ and K+ lower the affinity of whiting parvalbumin for Ca2+ and Mg2+ by almost an order of magnitude.
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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 |
Dec
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pubmed:issn |
0006-3002
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
749
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6652098-Animals,
pubmed-meshheading:6652098-Calcium,
pubmed-meshheading:6652098-Fishes,
pubmed-meshheading:6652098-Magnesium,
pubmed-meshheading:6652098-Muscle Proteins,
pubmed-meshheading:6652098-Parvalbumins,
pubmed-meshheading:6652098-Potassium,
pubmed-meshheading:6652098-Protein Binding,
pubmed-meshheading:6652098-Sodium,
pubmed-meshheading:6652098-Spectrometry, Fluorescence
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pubmed:year |
1983
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pubmed:articleTitle |
Sodium and potassium binding to parvalbumins measured by means of intrinsic protein fluorescence.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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