| pubmed-article:7525559 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7525559 | lifeskim:mentions | umls-concept:C0071728 | lld:lifeskim |
| pubmed-article:7525559 | lifeskim:mentions | umls-concept:C0914594 | lld:lifeskim |
| pubmed-article:7525559 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7525559 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:7525559 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:7525559 | pubmed:issue | 44 | lld:pubmed |
| pubmed-article:7525559 | pubmed:dateCreated | 1994-11-29 | lld:pubmed |
| pubmed-article:7525559 | 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. | lld:pubmed |
| pubmed-article:7525559 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7525559 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7525559 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7525559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7525559 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7525559 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7525559 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7525559 | pubmed:author | pubmed-author:BrdiczkaDD | lld:pubmed |
| pubmed-article:7525559 | pubmed:author | pubmed-author:WallimannTT | lld:pubmed |
| pubmed-article:7525559 | pubmed:author | pubmed-author:KaldisPP | lld:pubmed |
| pubmed-article:7525559 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7525559 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:7525559 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:7525559 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7525559 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7525559 | pubmed:pagination | 27640-4 | lld:pubmed |
| pubmed-article:7525559 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7525559 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7525559 | pubmed:articleTitle | In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. | lld:pubmed |
| pubmed-article:7525559 | pubmed:affiliation | Faculty of Biology, University of Konstanz, Germany. | lld:pubmed |
| pubmed-article:7525559 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7525559 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7525559 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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