The activities (Vmax) of hexokinase, glycogen phosphorylase, glucose-6-
phosphate dehydrogenase, phosphofructokinase, lactate dehydrogenase, citrate synthase,
cytochrome c oxidase, and 3-OH-acyl-CoA dehydrogenase in human skeletal muscles were
compared with the in vitro utilization of glucose and palmitic acid assessed under optimal
conditions. Statistically significant correlations between substrate fluxes and enzyme activities
were found suggesting that the substrate incorporation rate in vitro in some way
reflects the capacity of metabolic pathways. The incorporation rate of leucine into muscle
proteins was also statistically significantly correlated to the RNA concentration in the
muscle tissue.
Glycolytic and glycogenolytic enzymes correlated significantly to each other and correlations
were also found between aerobic enzymes supporting the validity of constant
proportions between certain key enzymes in human skeletal muscles.