scholarly journals Purification and Properties of White Muscle Lactate Dehydrogenase from the Anoxia-Tolerant Turtle, the Red-Eared Slider, Trachemys scripta elegans

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Neal J. Dawson ◽  
Ryan A. V. Bell ◽  
Kenneth B. Storey
Keyword(s):  
Lactate Dehydrogenase ◽  
White Muscle ◽  
Glycolytic Flux ◽  
Dot Blot ◽  
Muscle Lactate ◽  
Physiological Consequence ◽  
Ldh Activity ◽  
Purification And Properties ◽  
Dot Blot Analysis ◽  
Stimulation Of

Lactate dehydrogenase (LDH; E.C. 1.1.1.27) is a crucial enzyme involved in energy metabolism in muscle, facilitating the production of ATP via glycolysis during oxygen deprivation by recycling NAD+. The present study investigated purified LDH from the muscle of 20 h anoxic and normoxic T. s. elegans, and LDH from anoxic muscle showed a significantly lower (47%) Km for L-lactate and a higher Vmax value than the normoxic form. Several lines of evidence indicated that LDH was converted to a low phosphate form under anoxia: (a) stimulation of endogenously present protein phosphatases decreased the Km of L-lactate of control LDH to anoxic levels, whereas (b) stimulation of kinases increased the Km of L-lactate of anoxic LDH to normoxic levels, and (c) dot blot analysis shows significantly less serine (78%) and threonine (58%) phosphorylation in anoxic muscle LDH as compared to normoxic LDH. The physiological consequence of anoxia-induced LDH dephosphorylation appears to be an increase in LDH activity to promote the reduction of pyruvate in muscle tissue, converting the glycolytic end product to lactate to maintain a prolonged glycolytic flux under energy-stressed anoxic conditions.

scholarly journals Relationship between ontogenetic changes in foraging ecology and muscle lactate dehydrogenase activity in wild smallmouth bass (Micropterus dolomieu)

2016 ◽  
Vol 73 (9) ◽  
pp. 1389-1394 ◽  
Author(s):  
Frédéric Laberge ◽  
Nicholas Edmunds ◽  
Irene Yin-Liao ◽  
Kevin S. McCann
Keyword(s):  
Body Size ◽  
Lactate Dehydrogenase ◽  
Foraging Ecology ◽  
Trophic Position ◽  
Smallmouth Bass ◽  
Diet Shift ◽  
Micropterus Dolomieu ◽  
Muscle Lactate ◽  
Lactate Dehydrogenase Activity ◽  
Ldh Activity

The activity of muscle glycolytic enzymes scales positively with body size in active fish, a phenomenon thought to counter the increased costs of burst swimming faced by larger individuals. Recent work argued that changes in these enzymes during ontogeny additionally reflect changes in foraging ecology. Here, we evaluated the relationship between muscle anaerobic metabolism and foraging ecology in a population of wild smallmouth bass (Micropterus dolomieu) by relating activity of muscle lactate dehydrogenase (LDH) to estimates of trophic position and habitat use obtained from stable isotope signatures. As expected, LDH activity increased with body size. However, further analysis showed associations between foraging ecology and LDH activity. Specifically, a shift to higher trophic position, indicating a change in diet, was paralleled by a shift to increased LDH activity. However, a steady mass-specific decrease in LDH activity was observed as the fish grew above the size associated with this diet shift. Further, lower LDH activity was associated with increasing use of littoral carbon sources. These findings contribute to our understanding of how plasticity in muscle anaerobic potential is associated with fish foraging ecology.

scholarly journals Kinetic Studies of Rabbit Muscle Lactate Dehydrogenase

1962 ◽  
Vol 237 (5) ◽  
pp. 1668-1675
Author(s):  
Virginia Zewe ◽  
Herbert J. Fromm
Keyword(s):  
Lactate Dehydrogenase ◽  
Kinetic Studies ◽  
Rabbit Muscle ◽  
Muscle Lactate

scholarly journals Evaluation of equilibrium constants for the interaction of lactate dehydrogenase isoenzymes with reduced nicotinamide-adenine dinucleotide by affinity chromatography

1975 ◽  
Vol 151 (3) ◽  
pp. 631-636 ◽  
Author(s):  
R I Brinkworth ◽  
C J Masters ◽  
D J Winzor
Keyword(s):  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Equilibrium Constants ◽  
Mouse Tissue ◽  
Rabbit Muscle ◽  
Muscle Lactate ◽  
Sodium Phosphate Buffer ◽  
A Value ◽  
Series Of Experiments ◽  
Reduced Nicotinamide Adenine Dinucleotide

Rabbit muscle lactate dehydrogenase was subjected to frontal affinity chromatography on Sepharose-oxamate in the presence of various concentrations of NADH and sodium phosphate buffer (0.05 M, pH 6.8) containing 0.5 M-NaCl. Quantitative interpretation of the results yields an intrinsic association constant of 9.0 × 104M−1 for the interaction of enzyme with NADH at 5°C, a value that is confirmed by equilibrium-binding measurements. In a second series of experiments, zonal affinity chromatography of a mouse tissue extract under the same conditions was used to evaluate assoication constants of the order 2 × 105M−1, 3 × 105M−1, 4 × 105M−1, 7 × 105M−1 and 2 × 106M−1 for the interaction of NADH with the M4, M3H, M2H2, MH3 and H4 isoenzymes respectively of lactate dehydrogenase.

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