John Duncan, M.Sc. Biology 1988

Role of enzyme binding in muscle metabolism of the goldfish



Regulation of glycolytic metabolism in muscle by the reversible association of enzymes with the particulate fraction of the cell was assessed in heart and white skeletal muscle of the goldfish Carassius auratus. Three physiological states were compared: rested aerobic controls, 21 h of anoxia exposure in water bubbled with N2 and CO, and exhaustive swimming. Heart muscle responded to the anoxia exposure with an increase in the percentage bound for phosphofructokinase (PFK), aldolase, and pyruvate kinase, the greatest increase being for PFK (from 35 to 48%). When fish swam to exhaustion, however, no changes in the percentage bound occurred for the eight enzymes assayed in heart. In white muscle neither anoxia nor exhaustive swimming altered the binding of the eight enzymes to the particulate fraction of the cell, except for a significant decrease in the percentage of alcohol dehydrogenase bound in anoxic muscle. PFK binding was particularly high in white muscle (63-72% bound, assessed by two methods). PFK binding was sensitive to pH in both organs, with binding increasing as pH decreased. This suggests that binding of PFK could be enhanced when metabolism is highly dependent on glycolytic ATP production due to the fall in cellular pH as a result of metabolic acidosis.