Actomyosin ATPase, Myokinase, CPK and LDH in Human Fast and Slow Twitch Muscle Fibres

Abstract

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 fibers. The ratio in enzyme activity between fiber types was greatest for Mg2+ stimulated ATPase (3:1) and smallest for CPK (1.3:1). The isozyme patterns of CPK, MK and LDH were studied by means of isoelectric focusing (CPK and MK) and disc electrophoresis (LDH). A difference was observed between fiber types with respect to the isozyme distribution of MK and LDH, whereas the CPK isozyme pattern was similar in both fiber types. These results on separated human FT and ST fibers were essentially in conformity with what has earlier been indicated from experiments on mixed muscle homogenates.