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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1987-6-5
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pubmed:abstractText |
The single cysteine on the alpha-subunit of bovine brain S-100a protein has been modified with the thiol specific probe, Acrylodan. When the labelled apoprotein was excited at 380 nm the fluorescence emission maximum was centered at 484 +/- 2 nm, suggesting that the probe is in a fairly hydrophobic environment. Addition of Ca2+ to the protein caused the emission maximum to undergo a red shift to 504 +/- 2 nm, implying that the fluorophore is now more exposed to the solvent. Zn2+, when added to the protein, induced only a small perturbation and the emission maximum shifted to 481 +/- 2 nm. Ca2+ was able to perturb the fluorophore in the presence of Zn2+. 2-p-Toluidinylnaphthalene-6-sulfonate (TNS)-labelled alpha-subunit when excited at 345 nm exhibited very little fluorescence in the absence of Ca2+. Addition of Ca2+ resulted in an increase in TNS fluorescence accompanied by a blue shift of the emission maximum to 445 +/- 1 nm indicating that the probe in the presence of Ca2+ moves to a hydrophobic domain. The fact that Ca2+ and Zn2+ can perturb the labelled sulfhydryl group in the presence of each other clearly demonstrates that the binding sites for the two metal ions must be different on the alpha-subunit as well as on the S-100a protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-(4-toluidino)-6-naphthalenesulfoni...,
http://linkedlifedata.com/resource/pubmed/chemical/2-Naphthylamine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Naphthalenesulfonates,
http://linkedlifedata.com/resource/pubmed/chemical/S100 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/acrylodan
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
214
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3569515-2-Naphthylamine,
pubmed-meshheading:3569515-Animals,
pubmed-meshheading:3569515-Binding Sites,
pubmed-meshheading:3569515-Brain,
pubmed-meshheading:3569515-Calcium,
pubmed-meshheading:3569515-Cattle,
pubmed-meshheading:3569515-Cysteine,
pubmed-meshheading:3569515-Naphthalenesulfonates,
pubmed-meshheading:3569515-S100 Proteins,
pubmed-meshheading:3569515-Spectrometry, Fluorescence,
pubmed-meshheading:3569515-Zinc
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pubmed:year |
1987
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pubmed:articleTitle |
Fluorescence studies on the Ca2+ and Zn2+ binding properties of the alpha-subunit of bovine brain S-100a protein.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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