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lactate dehydrogenase/kartoffel
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A comparison of potato and vertebrate lactate dehydrogenases.
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A 2000-fold purification of L(+)-lactate dehydrogenase from potatoes is reported. Five isoenzymes of lactate dehydrogenase can be detected in crude extracts of potato, and three of these are present in the purified preparation. The enzyme (mol.wt. 150 000), which is composed of four subunits
Partial purification and characterization of L-lactate dehydrogenase isozymes from sweet potato roots.
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Lactate dehydrogenase [L-lactate: NAD oxidoreductase, EC 1.1.1.27] was isolated from sweet potato root tissues. Two species of the enzyme (isozymes I and II) were separated by DE-52 cellulose column chromatography from healthy, cut, and black-rot diseased tissues. Isozymes I and II were purified
Mitochondria isolated from local market potato tubers contain L-lactate dehydrogenase in an inactive state.
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In order to gain some insight into metabolism of mitochondria isolated from materials subjected to storage treatments, we compared mitochondria isolated from potato tubers grown and stored in the post-harvest without any chemicals (N-PTM), and tubers, from local market, treated for commercial
Characterization of potato (Solanum tuberosum)lactate dehydrogenase isoenzymes by affinity chromatography and hybridization.
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The five isoenzymes of potato (Solanum tuberasum) lactate dehydrogenase have been resolved by affinity chromatography. Mixtures of isoenzymes LDH-1 and LDH-5 dissociate and reassociate during freezing and thawing to produce five isoenzymes. These results indicate that potato lactate dehydrogenase
Purification and properties of L(+)-lactate dehydrogenase from potato tubers.
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1. A purification of l(+)-lactate dehydrogenase is described. 2. The final preparation is active with NADH and NADPH and with a number of keto acids, but evidence is presented to support the view that a single enzyme is involved. 3. NAD(+) showed product inhibition, but at slightly acid pH values
Affinity chromatography of potato lactate dehydrogenase [proceedings].
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Catalytic properties of three lactate dehydrogenases from potato tubers (Solanum tuberosum).
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Distribution of lactate dehydrogenase isoenzymes in potato (Solanum tuberosum) and other plants.
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Red potato extract protects from D-galactosamine-induced liver injury in rats.
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The protective effects of red potato extract (RPE) as to liver damage were determined in D-galactosamine (GalN)-intoxicated rats. Increases in serum aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase activities, all of which were induced by GalN injection, decreased in
Effects of Potato Cultivars on Some Physiological Processes of Leptinotarsa decemlineata (Coleoptera: Chrysomelidae).
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Colorado potato beetle, Leptinotarsa decemlineata (Say), is an important pest of potato throughout the world. Here, the effects of six potato cultivars including 'Arinda,' 'Sprit,' 'Markiez,' 'Lotta,' 'Santae,' and 'Agria' were studied on nutritional indices, digestive enzymes, and some components
The physiological role of the isoenzymes of lactate dehydrogenase in potatoes.
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Four of the five isoenzymes of lactate dehydrogenase present in potato tubers have been isolated and their kinetic properties examined. The pyruvate-reductase activity of isoenzyme-4 is greatly reduced at low pH, the affinity for both pyruvate and NADH is reduced and ATP has a stronger inhibitory
Hepatoprotective effects of purple potato extract against D-galactosamine-induced liver injury in rats.
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We investigated the hepatoprotective effect of purple potato extract (PPE) against D-galactosamine (GalN)-induced liver injury in rats. PPE (400 mg) was administered once daily for 8 d, and then GalN (250 mg/kg of body weight) was injected at 22 h before the rats were killed. Serum tumor necrosis
[Protective effect of purple sweet potato flavonoids on CCL4-induced acute liver injury in mice].
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OBJECTIVE
To investigate the protective effect of purple sweet potato flavonoids (PSPF) on CCl4-induced acute liver injury in mice.
METHODS
Sixty mice were randomly divided into six groups (n=10 in each): blank group, model group, PSPF groups (400 mg*kg(-1), 200 mg*kg-1 and 100 mg*kg(-1)) and
L-lactate metabolism in potato tuber mitochondria.
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We investigated the metabolism of L-lactate in mitochondria isolated from potato tubers grown and saved after harvest in the absence of any chemical agents. Immunologic analysis by western blot using goat polyclonal anti-lactate dehydrogenase showed the existence of a mitochondrial lactate
Purification and properties of hypoxically induced lactate dehydrogenase from barley roots.
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Using Affigel Blue and oxamate-agarose affinity chromatography, lactate dehydrogenase (LDH) was purified 2000-fold from hypoxically induced barley roots. Molecular weights of the native and sodium dodecyl sulfate-denatured LDH protein were 157 and 40 kilodaltons, respectively, indicating a tetramer.
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