Effect of temperature on the red and white muscle lactate dehydrogenase of thermally acclimated goldfish

1982 ◽  
Vol 73 (3) ◽  
pp. 607-611 ◽  
Author(s):  
Hiroko Tsukuda
Keyword(s):  
Lactate Dehydrogenase ◽  
White Muscle ◽  
Effect Of Temperature ◽  
Muscle Lactate

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 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.

Effects of Early Severe Malnutrition on Heart and Skeletal Muscle Lactate Dehydrogenase

1976 ◽  
Vol 106 (9) ◽  
pp. 1235-1240 ◽  
Author(s):  
David Penney ◽  
Debra Anderson ◽  
John Dongas
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Severe Malnutrition ◽  
Muscle Lactate
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