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malate/atrophy

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Leht 1 alates 111 tulemused

Glutamate and malate dehydrogenase activities in Joseph disease and olivopontocerebellar atrophy.

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The activities of brain glutamate dehydrogenase and malate dehydrogenase were not statistically different in samples from patients with autosomal dominant olivopontocerebellar atrophy or Joseph disease compared with control subject samples. These two enzymes are thus not involved in the pathogenesis

Acetyl-CoA synthetase, NADP malate dehydrogenase and ATP citrate lyase in the degenerating peripheral nerve.

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Increased brain and CSF lactate have been described in human and experimental portal-systemic encephalopathy (PSE). Using a recently described cisterna magna catheter technique, CSF lactate was measured in relation to deterioration of neurological status in portacaval shunted rats administered
In this study, we evaluated the fungicide effect on the incidence of rot grains and expression of catalase (CAT), alcohol dehydrogenase (ADH), and malate dehydrogenase (MDH) enzymes in commercial maize hybrids grown with conventional and reduced spacing in Guarapuava, PR, Brazil. The experiment was

Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii.

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Mitochondrial malate dehydrogenase (m-MDH; EC 1.1.1.37), from mycelial extracts of the thermophilic, aerobic fungus Talaromyces emersonii, was purified to homogeneity by sequential hydrophobic interaction and biospecific affinity chromatography steps. Native m-MDH was a dimer with an apparent

Controlled atmospheres and sugar can delay malate synthase gene expression during asparagus senescence

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A cDNA clone encoding malate synthase (MS; EC 4.1.3.2) was isolated from a 48-h postharvest asparagus (Asparagus officinalis L.) spear cDNA library using a MS clone from Brassica napus. The asparagus MS (AoMS1) cDNA hybridized to a 1.9-kb transcript that increased in abundance preferentially in

[Structure-activity features of malate dehydrogenase from human myocardium in atherosclerosis].

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A homogeneous preparation of malate dehydrogenase was obtained from human myocardium, the enzyme structure-functional properties were studied. Alterations in structure characteristics of the enzyme, increase in its hydrophobic moiety, decrease of the enzyme activity were observed during impairments
Conquering rapid postripeness and deterioration of Agaricus bisporus is quite challenging. We previously observed that methyl jasmonate (MeJA) pretreatment postponed the deterioration of A. bisporus, but the mechanism is unknown. Here, a nontargeted metabolomics analysis by
The evolutionary history of the malate dehydrogenase (MDH) gene family [NAD-dependent MDH; EC 1.1.1.37 and NAD(P)-dependent MDH; EC 1.1.1.82] has received much attention. MDHs have also featured extensively as electrophoretic markers in population genetics and evolutionary ecology, and in many
Daily administration of 2g/kg/day di(2-ethylhexyl)phthalate (DEHP) to immature rats was found to cause testicular atrophy and reduce zinc concentration. Specific activities of testicular enzymes associated with postmeiotic spermatogenic cells, such as lactate dehydrogenase isozyme-X, hyaluronidase
The loss of muscle weight in the soleus (SOL) and extensor digitorum longus (EDL) muscles was compared after denervation and in the course of reflex muscle atrophy induced by unilateral fracture of metatarsal bones of the paw and local injection of 0.02 ml turpentine oil subcutaneously. This
Enzyme activities of the energy supplying metabolism were investigated in muscle specimens of brachial biceps, deltoid or anterior tibial muscles of patients with traumatic nerve lesions, polyneuropathies, Charcot-Marie-Tooth disease, amyotrophic lateral sclerosis, spinal muscular atrophy and
UNASSIGNED Human studies on low-dose resveratrol are scarce. This study aims to evaluate the safety, tolerability, and efficacy of an oral preparation of resveratrol, glucose, and malate (RGM) in slowing the progression of Alzheimer's disease (AD). UNASSIGNED Thirty-nine subjects with mild to
Experiments for quantifying the amplitudes of motion of methyl-containing side chains are presented that exploit the rich network of cross-correlated spin relaxation interactions between intra-methyl dipoles in highly deuterated, selectively 13CH2D- or 13CH3-labeled proteins. In particular, the
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