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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-9-12
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pubmed:abstractText |
The purification of the channel-forming component of the mitochondrial calcium uniporter and its channel properties are described. After ethanol and 50% ethanol-water extraction of mitochondria from beef heart or perfused rat liver, the extract was passed through thiopropyl-Sepharose 6B column, and absorbed components were eluted with 2-mercaptoethanol, followed by gel-filtration on Sephadex G-15. The last fraction eluted (M(r) about 2000) was then subjected to reverse-phase high-performance liquid chromatography. Of the more than 10 distinct peaks, only one showed specific Ca(2+)-channel activity in BLM with properties similar to earlier, less extensively purified preparations, i.e., conductance of 20 pS and multiples thereof, clustering of channels, participation of 2 or more subunits in channel formation, and sensitivity to 1 microM ruthenium red. Voltage sensitivity and cooperativity between channels are described. The Ca(2+)-binding glycoprotein with which the peptide was associated was found to have high homology with human acid alpha 1-glycoprotein (orosomucoid) and to show identity with beef plasma orosomucoid in the Ouchterlony immunodiffusion test.
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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/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Orosomucoid,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial calcium uniporter
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0145-479X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
231-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8056790-Amino Acid Sequence,
pubmed-meshheading:8056790-Animals,
pubmed-meshheading:8056790-Calcium Channels,
pubmed-meshheading:8056790-Calcium-Binding Proteins,
pubmed-meshheading:8056790-Cattle,
pubmed-meshheading:8056790-Humans,
pubmed-meshheading:8056790-Immunochemistry,
pubmed-meshheading:8056790-Lipid Bilayers,
pubmed-meshheading:8056790-Mitochondria,
pubmed-meshheading:8056790-Mitochondria, Heart,
pubmed-meshheading:8056790-Mitochondria, Liver,
pubmed-meshheading:8056790-Molecular Sequence Data,
pubmed-meshheading:8056790-Orosomucoid,
pubmed-meshheading:8056790-Peptides,
pubmed-meshheading:8056790-Rats,
pubmed-meshheading:8056790-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
Purification of the channel component of the mitochondrial calcium uniporter and its reconstitution into planar lipid bilayers.
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pubmed:affiliation |
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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