Activities of malate dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase and fructose-1,6-diphosphatase with regard to metabolic subpopulations of fast- and slow-twitch fibres in rabbit muscles
- 1 January 1979
- journal article
- research article
- Published by Springer Nature in Histochemistry and Cell Biology
- Vol. 60 (1), 9-19
- https://doi.org/10.1007/bf00495725
Abstract
Activities of malate dehydrogenase (MDH), 3-hydroxyacyl-CoA dehydrogenase (HAD) and fructose-1,6-diphosphatase (FDPase) were determined in single fibres dissected from freeze-dried rabbit psoas and soleus muscles. Slow-twitch fibres as determined by qualitative ATPase reaction represent a rather uniform population with regard to HAD and MDH activities. In these fibres the two enzymes are in constant proportions. FDPase is found at extremely low activities in slow-twitch fibres and because of its relatively high activity in fast-twitch fibres of soleus and psoas muscle it might be used as a marker enzyme. Fast-twitch fibres in psoas muscle represent a heterogeneous population with regard to activities of MDH as well as of HAD. The two enzyme activities are not proportional in fasttwitch psoas fibres. These findings suggest the existence of metabolic sub-populations of fast-twitch fibres having a wide range of aerobic oxidative capacities and having differences in their capacity to oxidizing fatty acids.This publication has 21 references indexed in Scilit:
- Metabolic Characteristics of Fibre Types in Human Skeletal MuscleActa Physiologica Scandinavica, 1975
- Effects of long-term electrical stimulation on some contractile and metabolic characteristics of fast rabbit musclesPflügers Archiv - European Journal of Physiology, 1973
- Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbitsBiochemistry, 1972
- Comparative aspects of mitochondria isolated from αW, αR, and βR muscle fibers of the chickExperimental Neurology, 1972
- Adaptation of muscle to exerciseJournal of Clinical Investigation, 1971
- Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic OrganizationEuropean Journal of Biochemistry, 1969
- QUANTITATIVE HISTOCHEMICAL ANALYSIS OF GLYCOLYTIC INTERMEDIATES AND COFACTORS WITH AN OIL WELL TECHNIQUEJournal of Histochemistry & Cytochemistry, 1968
- THE OXIDATION OF LACTATE AND α-GLYCEROPHOSPHATE BY RED AND WHITE SKELETAL MUSCLE: I. QUANTITATIVE STUDIESJournal of Histochemistry & Cytochemistry, 1963
- Proportionskonstante Gruppen in Beziehung zur Differenzierung der Enzymaktivitätsmuster von Skelett-Muskeln des KaninchensHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1963
- Direct Relationship of Phosphorylase and Mitochondrial α-Glycerophosphate Dehydrogenase Activity in Skeletal MuscleNature, 1961