The effect of fatigue on the binding of glycolytic enzymes in the isolated gastrocnemius of Rana pipiens.
Fatigue of isolated gastrocnemius muscles from R. pipiens leads to a marked increase in the proportion of phosphofructokinase bound to the particulate fraction and a decrease in the binding of lactate dehydrogenase, pyruvate kinase, creatine phosphokinase and glyceraldehyde-3-phosphate dehydrogenase. Only the proportion of aldolase bound to the particulate fraction was unaffected by fatigue. This pattern was unchanged when fatigued muscles were extracted at pH 6.5 rather than 7.5. Thus, muscle fatigue leads to opposite changes in the binding of the glycolytic enzymes.
Guderley
H
H
Département de biologie, Université Laval, Québec, Canada.
Jean
C
C
Blouin
M
M
D000818:Animals; D003402:Creatine Kinase / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D006019:Glycolysis; D066298:In Vitro Techniques; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D009132:Muscles / Q000201:enzymology / Q000502:physiology*; D011485:Protein Binding; D011770:Pyruvate Kinase / Q000378:metabolism; D011894:Rana pipiens
D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011770:Pyruvate Kinase; D003402:Creatine Kinase; D005634:Fructose-Bisphosphate Aldolase