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Actomyosin ATPase, myokinase, CPK and LDH in human fast and slow twitch muscle fibres.
Swedish School of Sport and Health Sciences, GIH, Department of Sport and Health Sciences, Laboratory for Biomechanics and Motor Control.
1977 (English)In: Acta Physiologica Scandinavica, ISSN 0001-6772, E-ISSN 1365-201X, Vol. 99, no 2, 225-9 p.Article in journal (Refereed) Published
Abstract [en]

The enzyme activities of Mg2+ stimulated ATPase, creatine phosphokinase (CPK), myokinase (MK) and lactate dehydrogenase (LDH) were determined in pooled fast twitch (FT) and slow twitch (ST) human skeletal muscle fibers, dissected out from freeze-dried muscle biopsy material. All enzymes investigated demonstrated higher activities in FT fibres. The ratio in enzyme activity between fibre types was greatest for Mg2+ stimulated ATPase (3:1) and smallest for CPK (1.3:1). In addition, the isozyme patterns of CPK, MK and LDH were studied by means of isoelectric focusing (CPK and MK) and discelectrophoresis (LDH). A difference was observed between fibre types with respect to the isozyme distribution of MK and LDH, whereas the CPK isozyme pattern was similar in both fibre types. These results on separated human FT and ST fibres were essentially in conformity with what has earlier been indicated from experiments on mixed muscle homogenates.

Place, publisher, year, edition, pages
1977. Vol. 99, no 2, 225-9 p.
Identifiers
URN: urn:nbn:se:gih:diva-619PubMedID: 190869OAI: oai:DiVA.org:gih-619DiVA: diva2:173825
Available from: 2009-02-17 Created: 2009-02-16 Last updated: 2011-05-03Bibliographically approved

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