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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
1990-10-11
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pubmed:abstractText |
In a recent study it has been shown that mitochondrial creatine kinase from chicken brain (Mia-CK) and heart (Mib-CK) are two distinct isoenzymes differing in ten out of the thirty N-terminal amino acids (Hossle, J.P., Schlegel, J., Wegmann, G., Wyss, M., Böhlen, P., Eppenberger, H.M., Wallimann, T., and Perriard J.C. (1988) Biochem. Biophys. Res. Commun. 151, 408-416). The present article describes the purification and biophysical characterization of the mitochondrial creatine kinase isoenzyme from chicken brain (Mia-CK). Gel permeation chromatography, direct mass measurements of individual molecules by scanning transmission electron microscopy, and analytical ultracentrifugation confirmed the existence of two different oligomeric forms, dimeric and octameric Mia-CK, with molecular masses of 85 kDa and 306-352 kDa and with sedimentation constants of 4.9-5.3 and 11.6-12.0 S, respectively. In addition, it was tested if Mia- and Mib-CK can form heterodimeric and heterooctameric molecules with subunits of other CK isoenzymes. By denaturation in urea or guanidine hydrochloride and subsequent renaturation, MiaMib-CK and surprisingly also MiaM-CK heterodimers could be generated. In contrast, no heterodimers were obtained between Mib- and M- or B-CK. Furthermore, reoctamerization of a mixture of Mia- and Mib-CK homodimers led to the formation of MiaMib-CK heterooctamers. In these heterooctamers, the Mia- and Mib-CK homodimers remained the fundamental building blocks. No subunit exchange between adjacent dimers within the heterooctamer could be observed even after storage for 3 months at 4 degrees C. The relevance of these data on the structural organization of the Mi-CK octamer and on the physiological aspects of tissue-specific isoenzyme expression are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15900-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2394753-Amino Acid Sequence,
pubmed-meshheading:2394753-Animals,
pubmed-meshheading:2394753-Brain,
pubmed-meshheading:2394753-Chickens,
pubmed-meshheading:2394753-Chromatography, Affinity,
pubmed-meshheading:2394753-Chromatography, Ion Exchange,
pubmed-meshheading:2394753-Creatine Kinase,
pubmed-meshheading:2394753-Humans,
pubmed-meshheading:2394753-Isoenzymes,
pubmed-meshheading:2394753-Kinetics,
pubmed-meshheading:2394753-Macromolecular Substances,
pubmed-meshheading:2394753-Mitochondria,
pubmed-meshheading:2394753-Molecular Sequence Data,
pubmed-meshheading:2394753-Molecular Weight,
pubmed-meshheading:2394753-Sequence Homology, Nucleic Acid
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pubmed:year |
1990
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pubmed:articleTitle |
Mitochondrial creatine kinase from chicken brain. Purification, biophysical characterization, and generation of heterodimeric and heterooctameric molecules with subunits of other creatine kinase isoenzymes.
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pubmed:affiliation |
Institute of Cell Biology, ETH Hönggerberg, Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Comparative Study
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