scholarly journals Affinity chromatography of lactate dehydrogenase on immobilized nucleotides

1973 ◽  
Vol 133 (3) ◽  
pp. 515-520 ◽  
Author(s):  
C. R. Lowe ◽  
P. D. G. Dean
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Heart Muscle ◽  
Adenine Nucleotides ◽  
Free Solution ◽  
Muscle Lactate ◽  
Effects Of Ph ◽  
Influence Of Substrate ◽  
Lactate Dehydrogenase Isoenzymes

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.

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

Unusual Variant of Lactate Dehydrogenase Isoenzymes

1975 ◽  
Vol 21 (1) ◽  
pp. 162-164 ◽  
Author(s):  
D H Buchholz ◽  
R K Donabedian
Keyword(s):  
Skeletal Muscle ◽  
Lymph Node ◽  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Genetic Locus ◽  
Negro Woman ◽  
Unusual Variant ◽  
Heterozygous Form ◽  
Monomeric Proteins ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Thirteen electrophoretic bands of lactate dehydrogenase isoenzyme activity were detected in the serum of a 69-year-old Negro woman who died of pseudomonas pneumonia. No evidence of tumor was found at necropsy, and additional studies of the enzymatic activity of crude extracts of liver, lung, spleen, kidney, brain, skeletal muscle, lymph node, and heart revealed 1, 2, 3, 4, and 5 separate isoenzyme bands for lactate dehydrogenase isoenzymes 1, 2, 3, 4, and 5, respectively (a total of 15 isoenzyme bands). Serum and erythrocyte hemolysate from one of two healthy daughters displayed a similar pattern of multiple isoenzyme bands in isoenzymes 2 and 3. The observed pattern is consistent with the heterozygous form of a mutation of the genetic locus controlling synthesis of the M monomer such that two differently charged monomeric proteins are produced, each of which apparently combines with H chains with equal facility, leading to the multiband enzymatic specificity seen.

Lactate dehydrogenase isoenzymes. Turnover in rat heart, skeletal muscle, and liver

Biochemistry ◽  
1973 ◽  
Vol 12 (21) ◽  
pp. 4034-4039 ◽  
Author(s):  
Paul J. Fritz ◽  
E. Lucile White ◽  
Kenneth M. Pruitt ◽  
Elliot S. Vesell
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Rat Heart ◽  
Lactate Dehydrogenase Isoenzymes
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