Biomimetic dye affinity chromatography for the purification of bovine heart lactate dehydrogenase

1995 ◽  
Vol 718 (1) ◽  
pp. 35-44 ◽  
Author(s):  
N.E. Labrou ◽  
Y.D. Clonis
Keyword(s):  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Bovine Heart ◽  
Dye Affinity Chromatography

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.

Polymer displacement in dye-affinity chromatography

1995 ◽  
Vol 710 (2) ◽  
pp. 259-266 ◽  
Author(s):  
Igor Yu. Galaev ◽  
Pär Arvidsson ◽  
Bo Mattiasson
Keyword(s):  
Affinity Chromatography ◽  
Dye Affinity Chromatography

Fungal pectic enzyme fractionation by dye affinity chromatography

1996 ◽  
Vol 10 (3) ◽  
pp. 211-214 ◽  
Author(s):  
Silvia A. Camperi ◽  
Mariano Grasselli ◽  
Osvaldo Cascone
Keyword(s):  
Affinity Chromatography ◽  
Pectic Enzyme ◽  
Dye Affinity Chromatography

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.

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