Simultaneous purification of L-malate dehydrogenase and L-lactate dehydrogenase from bovine heart by biomimetic-dye affinity chromatography

3-Hydroxybutyrate dehydrogenase (EC 1.1.1.30) and malate dehydrogenase (EC 1.1.1.37) were purified to homogeneity on a large scale involving only two sequential affinity-chromatography steps on two triazine dye-Sepharose matrices. Recoveries of both enzymes were in excess of 60%. Malate dehydrogenase could also be purified by a combination of triazine dye affinity chromatography and gel filtration on Ultrogel AcA-44, but this offered no significant advantage over the purely affinity procedure.

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Four Weeks of Aerobic Training Affects Cardiac Tissue Matrix Metalloproteinase, Lactate Dehydrogenase and Malate Dehydrogenase Enzymes Activities, and Hepatorenal Biomarkers in Experimental Hyperhomocysteinemia in Rats

International Journal of Molecular Sciences ◽

10.3390/ijms22136792 ◽

2021 ◽

Vol 22 (13) ◽

pp. 6792

Author(s):

Dusan Todorovic ◽

Marija Stojanovic ◽

Ana Medic ◽

Kristina Gopcevic ◽

Slavica Mutavdzin ◽

...

Keyword(s):

Physical Activity ◽

Lactate Dehydrogenase ◽

Malate Dehydrogenase ◽

Subcutaneous Injection ◽

Cardiac Tissue ◽

Albino Rats ◽

Wistar Albino Rats ◽

And Control ◽

Tissue Matrix ◽

Increased Activity

The aim of this study was to investigate the effect of the application of homocysteine as well as its effect under the condition of aerobic physical activity on the activities of matrix metalloproteinases (MMP), lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) in cardiac tissue and on hepato-renal biochemical parameters in sera of rats. Male Wistar albino rats were divided into four groups (n = 10, per group): C: 0.9% NaCl 0.2 mL/day subcutaneous injection (s.c.); H: homocysteine 0.45 µmol/g b.w./day s.c.; CPA saline (0.9% NaCl 0.2 mL/day s.c.) and a program of physical activity on a treadmill; and HPA homocysteine (0.45 µmol/g b.w./day s.c.) and a program of physical activity on a treadmill. Subcutaneous injection of substances was applied 2 times a day at intervals of 8 h during the first two weeks of experimental protocol. Hcy level in serum was significantly higher in the HPA group compared to the CPA group (p < 0.05). Levels of glucose, proteins, albumin, and hepatorenal biomarkers were higher in active groups compared with the sedentary group. It was demonstrated that the increased activities of LDH (mainly caused by higher activity of isoform LDH2) and mMDH were found under the condition of homocysteine-treated rats plus aerobic physical activity. Independent application of homocysteine did not lead to these changes. Physical activity leads to activation of MMP-2 isoform and to increased activity of MMP-9 isoform in both homocysteine-treated and control rats.

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Malate dehydrogenase and lactate dehydrogenase in snail (helix pomatia) foot muscle extract. Comparison of the activity with NADH and deamino-NADH

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(82)92110-6 ◽

1982 ◽

Vol 108 (3) ◽

pp. 1080-1084

Author(s):

Andrzej J. Stankiewicz

Keyword(s):

Lactate Dehydrogenase ◽

Malate Dehydrogenase ◽

Helix Pomatia ◽

Muscle Extract ◽

Snail Helix Pomatia

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

Biochemical Journal ◽

10.1042/bj1510631 ◽

1975 ◽

Vol 151 (3) ◽

pp. 631-636 ◽

Cited By ~ 32

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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