We are analyzing https://link.springer.com/article/10.1007/bf00763072.

Title:
Purification of the channel component of the mitochondrial calcium uniporter and its reconstitution into planar lipid bilayers | Journal of Bioenergetics and Biomembranes
Description:
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 Ca2+-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 µM ruthenium red. Voltage sensitivity and cooperativity between channels are described. The Ca2+-binding glycoprotein with which the peptide was associated was found to have high homology with human acid α1-glycoprotein (orosomucoid) and to show identity with beef plasma orosomucoid in the Ouchterlony immunodiffusion test.
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Keywords {🔍}

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Topics {✒️}

human acid α1-glycoprotein mitochondrial calcium uniporter month download article/chapter ca2+ ion interactions planar lipid bilayers thiopropyl-sepharose 6b column ca2+-binding glycoprotein beef plasma orosomucoid privacy choices/manage cookies channels related subjects full article pdf channel-forming component marc baumann european economic area perfused rat liver extensively purified preparations ouchterlony immunodiffusion test abi user bull proteins conditions privacy policy check access instant access accepting optional cookies 50% ethanol-water extraction journal finder publish main content log adgemurat berdimuratov voltage sensitivity channel component channel properties channel formation orosomucoid baumann article journal high homology latest articles russia galina privacy policy reconstitution personal data tatjana sirota purification books a oleg kolomytkin article log optional cookies manage preferences saris institute article mironova

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         description: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 Ca2+-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 µM ruthenium red. Voltage sensitivity and cooperativity between channels are described. The Ca2+-binding glycoprotein with which the peptide was associated was found to have high homology with human acid α1-glycoprotein (orosomucoid) and to show identity with beef plasma orosomucoid in the Ouchterlony immunodiffusion test.
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      dateModified:
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         black-lipid membrane
         calcium uniporter
         channel
         orosomucoid
         reconstitution
         Bioorganic Chemistry
         Biochemistry
         general
         Animal Anatomy / Morphology / Histology
         Animal Biochemistry
         Organic Chemistry
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