Use of p-aminophenyl D-and L-lactic acids and p-aminophenyl pyruvic acid as effectors in the affinity chromatography of lactate dehydrogenase

Biochimie ◽  
1979 ◽  
Vol 61 (3) ◽  
pp. 437-442 ◽  
Author(s):  
E. Brown ◽  
R. Joyeau
Keyword(s):  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Pyruvic Acid ◽  
Lactic Acids

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.

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.

A lactate dehydrogenase-immunoglobulin G1 complex, not blocked by anti-idiotype antibody, in a patient with IgG1-lambda type M-proteinemia.

1987 ◽  
Vol 33 (8) ◽  
pp. 1478-1483 ◽  
Author(s):  
K Fujita ◽  
I Sakurabayashi ◽  
M Kusanagi ◽  
T Kawai
Keyword(s):  
Lactate Dehydrogenase ◽  
Complex Formation ◽  
Affinity Chromatography ◽  
Binding Site ◽  
Binding Capacity ◽  
Isoenzyme Pattern ◽  
M Protein ◽  
Light Chains ◽  
Ldh Isoenzymes ◽  
Sepharose 4B

Abstract The serum of a patient with IgG1-lambda type M-proteinemia showed an abnormal isoenzyme pattern for lactate dehydrogenase (LDH, EC 1.1.1.27). By affinity chromatography, we showed that four isoenzymes (LDH2, LDH3, LDH4, and LDH5) were bound to the M-protein. This complex formation was not blocked by anti-idiotype antibody, even though the binding capacity of IgG was exclusively located in the Fab region of the molecule. Moreover, heavy and light chains of the patient's IgG, obtained by reduction, separately had affinities for each of the LDH isoenzymes. LDH-IgG complex was easily dissociated by affinity chromatography on 5'-AMP-Sepharose 4B or by added NADH. We propose the following hypothesis for the LDH-IgG complex formation: LDH can recognize the gamma-Fab region of IgG at the NAD+ binding site of the molecule, but the affinity of the LDH molecule for immunoglobulin is much weaker than that for NADH or 5'-AMP.

Affinity chromatography of rat liver lactate dehydrogenase on the Remazol derivative of bead cellulose

1980 ◽  
Vol 194 (1) ◽  
pp. 95-99 ◽  
Author(s):  
Danica Mislovičová ◽  
Peter Gemeiner ◽  
Ľudovít Kuniak ◽  
Jiří Zemek
Keyword(s):  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Rat Liver ◽  
Bead Cellulose
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