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  Creatine phosphokinase: isoenzymes in Torpedo marmorata

Witzemann, V. (1985). Creatine phosphokinase: isoenzymes in Torpedo marmorata. European Journal of Biochemistry, 150(1), 201-210. doi:10.1111/j.1432-1033.1985.tb09008.x.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0000-CF08-F Version Permalink: https://hdl.handle.net/21.11116/0000-0000-CF09-E
Genre: Journal Article

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 Creators:
Witzemann, Veit1, 2, 3, 4, Author           
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1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
3Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              
4Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: Creatine phosphokinase (ATP: creatine N-phosphotransferase, EC 2.7.3.2) is the major constituent of the "low-salt-soluble" proteins of the electric organ from Torpedo marmorata. The denatured subunits of the enzyme have an apparent Mr of 43 000 and isoelectric points ranging between pH 6.2 and pH 6.5. Identical properties are found for the creatine phosphokinase from Torpedo muscle tissue. Anti-(electric organ creatine phosphokinase) antibodies are specific for the muscle-type enzyme and do not cross-react with enzymes present in Torpedo brain and electric lobe tissue. Biochemical and immunochemical properties of the enzyme associated with acetylcholine-receptor-enriched membranes show that this enzyme is as the "low-salt-soluble" electric organ enzyme of the muscle-specific type. In vitro translation of electric organ poly(A)-rich mRNA in a reticulocyte lysate reveals the abundance of mRNA specific for muscle creatine phosphokinase. During embryonic development of the electrocyte a continuous increase of translatable amounts of this mRNA is observed. No brain-type polypeptides are synthesized. The subunits of the brain-specific enzyme differ in molecular mass (Mr approximately equal to 42000) and isoelectric properties (pI approximately equal to 7.0-7.2). The unexpected finding that the brain forms are more basic than the muscle-specific enzyme is supported by agarose and cellulose acetate electrophoresis and ion-exchange chromatography properties.

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Language(s): eng - English
 Dates: 1985-02-2619851985-07-01
 Publication Status: Issued
 Pages: 10
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 Rev. Type: Peer
 Identifiers: DOI: 10.1111/j.1432-1033.1985.tb09008.x
URI: https://www.ncbi.nlm.nih.gov/pubmed/4018079
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 150 (1) Sequence Number: - Start / End Page: 201 - 210 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040