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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1989-7-6
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pubmed:abstractText |
The persistence of proteins in a number of biological systems has been analyzed by density labeling techniques; however, the utility of this approach has been severely hampered by poor resolution between density-labeled and unlabeled proteins on equilibrium gradients. A high resolution equilibrium salt gradient composed of KSCN/CsSCN has been developed to effectively separate density-labeled proteins (13C-15N-2H-substituted) from unlabeled proteins. The resolution of this system is approximately twofold greater than that previously achieved with cesium formate/guanidine hydrochloride equilibrium gradients which have been used in many recent protein density labeling studies. In order to examine the extent of cross-contamination between density-labeled and unlabeled proteins in a KSCN/CsSCN gradient system, density-labeled chick epidermal proteins were mixed with unlabeled Drosophila larval proteins and then separated on these equilibrium gradients. From individual gradient fractions proteins were recovered and fractionated on a sodium dodecyl sulfate-polyacrylamide gel, demonstrating the virtually complete separation between the two populations. The general utility of this system for protein stability studies is also demonstrated.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Cesium,
http://linkedlifedata.com/resource/pubmed/chemical/Deuterium,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiocyanates,
http://linkedlifedata.com/resource/pubmed/chemical/potassium thiocyanate
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0003-2697
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
333-40
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2499216-Animals,
pubmed-meshheading:2499216-Carbon Isotopes,
pubmed-meshheading:2499216-Centrifugation, Density Gradient,
pubmed-meshheading:2499216-Cesium,
pubmed-meshheading:2499216-Chickens,
pubmed-meshheading:2499216-Deuterium,
pubmed-meshheading:2499216-Drosophila melanogaster,
pubmed-meshheading:2499216-Epidermis,
pubmed-meshheading:2499216-Indicators and Reagents,
pubmed-meshheading:2499216-Isotope Labeling,
pubmed-meshheading:2499216-Larva,
pubmed-meshheading:2499216-Nitrogen Isotopes,
pubmed-meshheading:2499216-Proteins,
pubmed-meshheading:2499216-Skin,
pubmed-meshheading:2499216-Thiocyanates
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pubmed:year |
1989
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pubmed:articleTitle |
High resolution KSCN/CsSCN equilibrium gradients effectively separate a population of density labeled proteins from unlabeled proteins.
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pubmed:affiliation |
Department of Biology, University of Virginia, Gilmer Hall, Charlottesville, 22901.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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