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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
44
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pubmed:dateCreated |
1994-11-29
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pubmed:abstractText |
An interaction of mitochondrial creatine kinase with purified outer mitochondrial porin (voltage-dependent anion channel) was shown by co-sedimentation assays as well as by gel permeation chromatography. Porin formed high M(r) complexes with wild-type mitochondrial creatine kinase as well as with an N-terminal deletion mutant, lacking the first five N-terminal amino acids. The complexes were identified by creatine kinase activity in parallel with immunoblotting using specific antibodies against the two proteins. In addition, porin induced octamerization of the N-terminal creatine kinase mutant, which under the same conditions without porin, did not polymerize but remained more than 90% dimeric. Furthermore, binding of mitochondrial creatine kinase to porin affected the conductance of porin when reconstituted in "black membranes." At 10 mV the pore in the complex adopted a low conductance (1.5-2 nanosiemens) state, compared to the high conductance state (3-4 nanosiemens) of the free incorporated pores. The former state of the pore is known to be cationically selective. Thus, besides a specific structural interaction, a defined physiological function is assumed of the mitochondrial creatine kinase-porin complexes that are discussed here.
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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/Creatine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/Voltage-Dependent Anion Channels
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27640-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7525559-Animals,
pubmed-meshheading:7525559-Creatine Kinase,
pubmed-meshheading:7525559-Electric Conductivity,
pubmed-meshheading:7525559-Ion Channels,
pubmed-meshheading:7525559-Lipid Bilayers,
pubmed-meshheading:7525559-Macromolecular Substances,
pubmed-meshheading:7525559-Membrane Proteins,
pubmed-meshheading:7525559-Mitochondria,
pubmed-meshheading:7525559-Porins,
pubmed-meshheading:7525559-Protein Binding,
pubmed-meshheading:7525559-Rats,
pubmed-meshheading:7525559-Sequence Deletion,
pubmed-meshheading:7525559-Structure-Activity Relationship,
pubmed-meshheading:7525559-Voltage-Dependent Anion Channels
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pubmed:year |
1994
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pubmed:articleTitle |
In vitro complex formation between the octamer of mitochondrial creatine kinase and porin.
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pubmed:affiliation |
Faculty of Biology, University of Konstanz, Germany.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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