SKELETAL MUSCLE LACTATE DEHYDROGENASE ISOENZYME ALTERATIONS IN MARATHON RUNNERS

1986 ◽  
Vol 18 (supplement) ◽  
pp. S89
Author(s):  
F. S. Apple ◽  
M. A. Rogers
1986 ◽  
Vol 61 (2) ◽  
pp. 477-481 ◽  
Author(s):  
F. S. Apple ◽  
M. A. Rogers

Total lactate dehydrogenase (LD) and LD isozyme activities in gastrocnemius muscle from trained men and women runners were measured in response to the chronic stress of training for a marathon race (42.2 km). Following 9 wk of training, total LD activity in skeletal muscle from men and women runners significantly (P less than 0.02) decreased 2.26 and 2.25 U/mg protein, respectively. However, men's total LD activities were significantly (P less than 0.001) less than the women's both before and after training. Significant (P less than 0.05) increases in LD1 activities in skeletal muscle in men and women runners were also observed after training. No significant correlations were detected between percent fiber type composition in men or women vs. the changes in total LD activity, changes in LD1 activity, maximal O2 consumption or training distance averaged per week after the training period. The biochemical adaptations in skeletal muscle that occurred in the LD isozyme composition in both men and women runners make the runners skeletal muscle appear similar to heart muscle in LD1 and LD2 activities.


1976 ◽  
Vol 106 (9) ◽  
pp. 1235-1240 ◽  
Author(s):  
David Penney ◽  
Debra Anderson ◽  
John Dongas

1973 ◽  
Vol 133 (3) ◽  
pp. 515-520 ◽  
Author(s):  
C. R. Lowe ◽  
P. D. G. Dean

The interaction of two isoenzymes of lactate dehydrogenase from pig heart muscle (H4) and rabbit skeletal muscle (M4), with immobilized nucleotides was examined: the effects of pH and temperature on the binding of lactate dehydrogenase were studied with immobilized NAD+ matrices. The influence of substrate, product and sulphite on the binding of heart muscle lactate dehydrogenase to immobilized NAD+ was investigated. The interaction of both lactate dehydrogenase isoenzymes with immobilized pyridine and adenine nucleotides and their derivatives were measured. The effects of these parameters on the interaction of lactate dehydrogenase with immobilized nucleotides were correlated with the known kinetic and molecular properties of the enzymes in free solution.


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