Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.37 (malate dehydrogenase)
 4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human adult lung fragments removed from macroscopically undamaged and anthracosis exempted zones of lungs of 20 pneumonectomies made for cancer, were tested for 25 enzymic activities. The location and intensities of these enzymic activities were different in the lung tissue components; The bronchial epithelia contained highly active LDH, MDH, SDH, NADH-TR and NADPH-TR, glucose-6-phosphate dehydrogenase, active hydroxyproline-2-epimerase, alkaline phosphatase. Ca2+-activated ATP-ase, and beta-galactosidase. Bronchial and vascular muscles presented intense activities of LDH, MDH and SDH of alkalinephosphatase, AMP-ase and Ca2+-activated ATP-ase, as well as of beta-galactosidase. The alveolar walls presented high activities of SDH, MDH and LDH, of alkaline and acid phosphatases, of beta-galactosidase and of Tween-40 and 60-esterases, of HEP, cytochrome-oxidase and peroxidase. The free alveolar macrophages were active for LDH, MDH, SDH, NADH-TR and NADPH-TR, G1-6-ph-DH, acid and alkaline phosphatase, cytochrome-oxidase and peroxidase, HEP, AMP-ase and Mg2+-activated ATP-ase, Tween-esterases, naphthol-ASD-acetate esterase, and beta-galactosidase. The endothelia contained high activities of alkaline phosphatase, of AMP-ase and Mg2+-activated ATPase, of LDH, MDH and SDH, and of beta-galactosidase. In bronchial lymphoid nodules it was the LDH, MDH, SDH, cytochrome-oxidase and peroxidase, HEP, alkaline phosphatase and AMP-ase, Tween-60-esterase and beta-galactosidase that were active. The interlobular areas of the lung presented intense activities of SDH, MDH, LDH, HEP and cytochrome-oxidase. The activities of the other tested enzymes were weaker or absent in the adult human lung components, the same as those of aminopeptidases which were present only in some free alveolar macrophages. The discussion of some relationships between these enzymic actitivies and the morphology of the human adult lung tissue asserted that the latter could not be considered as a "normal" tissue but as one overstrained by the components of blood and polluted air.
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PMID:Histoenzymology of the lung. I. Enzyme activities of the lung tissue of acult humans; relationships between structure and functions. 14 Mar 14

Eschscholtzia californica stigmas with germinating pollen at different stages of development were the subject of histochemical studies which aimed the localization of several enzymes like phosphorylase, leucine amino peptidase, nonspecific esterase, cytochrome oxidase, aldolase, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, monoamine oxidase, alpha-galactosidase, beta-glucosidase and beta-galactosidase. Pollen and pollen tubes were shown to contain starch, lipid, proteins and soluble sugars as the storage products. These storage products were utilized during germination and tube growth. The role of different enzymes in the process of germination and tube growth is discussed. From the distribution of oxidoreductases it is inferred that respiration plays an essential role in the tube growth. During pollen germination probably the reserve proteins were transported to pollen tube tip. The increase of activity of alpha-and beta-galactosidase in pollen tubes indicates on their involvement in carbohydrate metabolism. The role of alpha-galactosidase in the metabolism of galactolipids is also inferred. Similarly, the reaction catalysed by beta-glucosidase resulted in the production of aglycon and glucose; of these the former possibly act as a substrate of peroxidase. Some of the glycosidases diffused out of pollen wall on the stigma and participated in the release of free sugars of the female tissue.
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PMID:Studies on the physiology of pollen and pollen tube growth. IV Eschscholtzia californica Cham. 22 Jan 58

Cell-wall enzymes were assayed by the difference between enzyme activities in the whole cell and the protoplast. Both peroxidase (85.2%) and acid phosphatase (21.9%) were located in the wall. However, malate dehydrogenase was found only in the protoplast. A study of the time-course of the release of peroxidase and malate dehydrogenase into the incubation medium from cells either treated with cellulase or untreated, also indicated that peroxidase and not malate dehydrogenase was located in the wall. Only two anodic isoenzymes of peroxidase were present in the cell wall. These were more negatively charged than those of horseradish peroxidase.
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PMID:Some enzymes present in the walls of mesophyll cells of tobacco leaves. 121 11

Ubiquinol-1 in aerated aqueous solution inactivates several enzymes--alanine aminotransferase, alkaline phosphatase, Na+/K(+)-ATPase, creatine kinase and glutamine synthetase--but not isocitrate dehydrogenase and malate dehydrogenase. Ubiquinone-1 and/or H2O2 do not affect the activity of alkaline phosphatase and glutamine synthetase chosen as model enzymes. Dioxygen and transition metal ions, even if in trace amounts, are essential for the enzyme inactivation, which indeed does not occur under argon atmosphere or in the presence of metal chelators. Supplementation with redox-active metal ions (Fe3+ or Cu2+), moreover, potentiates alkaline phosphatase inactivation. Since catalase and peroxidase protect while superoxide dismutase does not, hydrogen peroxide rather than superoxide anion seems to be involved in the inactivation mechanism through which oxygen active species (hydroxyl radical or any other equivalent species) are produced via a modified Haber-Weiss cycle, triggered by metal-catalyzed oxidation of ubiquinol-1. The lack of efficiency of radical scavengers and the almost complete protection afforded by enzyme substrates and metal cofactors indicate a 'site-specific' radical attack as responsible for the oxidative damage.
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PMID:Enzyme inactivation by metal-catalyzed oxidation of coenzyme Q1. 135 46

When plant tissue extracts are electrophoresed on polyacrylamide gels and the gels are stained for malate dehydrogenase by the standard NAD-dependent dehydrogenase reaction, terminating in the formation of reduced Nitroblue Tetrazolium (NBT), achromatic bands, in addition to the expected chromatic bands, are observed. The achromatic bands are seen when the staining conditions favor a generalized background staining of the gel and have been shown, in a previous study, to be caused by peroxidase isozymes [1]. The present study examined the mechanism by which peroxidase produced the achromatic bands using horseradish peroxidase (HRP). The generalized background staining resulted from the phenazine methosulfate (PMS)-mediated reduction of NBT. This reduction was enhanced by H2O2 and suppressed by HRP. Peroxidase apparently catalyzes the peroxidative oxidation of reduced PMS, which suppresses the generalized reduction of NBT in gel regions containing peroxidase isozymes producing the achromatic bands. In contrast, however, HRP also appears to catalyze the peroxidative oxidation of reduced NAD, but this reaction increases the reduction of NBT. The results are discussed in the context of the mechanisms proposed by others for the PMS-mediated reduction of NBT and for the peroxidase-catalyzed NADH-dependent formation of H2O2. This peroxidase-catalyzed reaction has been proposed for the plant peroxidases involved in lignification.
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PMID:An explanation of the achromatic bands produced by peroxidase isozymes in polyacrylamide electrophoresis gels stained for malate dehydrogenase. 137 53

The proteins of soybean roots undergoing anaerobiosis can be grouped into three classes. Class 1 proteins are induced severalfold and at least 28 of these were identified by in vivo labeling. These proteins include the enzymes alcohol dehydrogenase (ADH), fructose aldolase, pyruvate decarboxylase, phosphoglucomutase, and lactate dehydrogenase. Class 2 proteins include such enzymes as glucose phosphate isomerase, sucrase, and malate dehydrogenase; their specific activity remains constant in aerobiosis or anaerobiosis. The third class of proteins includes those enzymes such as peroxidase whose activity decreases more than 90% after just 1 day in anaerobiosis. Immunoblotting coupled with two-dimensional chromatography of in vitro translated plant extracts demonstrated that ADH level during anaerobiosis is controlled by its mRNA concentration. Little or no mRNA for ADH was detected in aerobically grown roots. This suggests that the increased level of ADH activity is due to de novo synthesis of the mRNA rather than activation of a sequestered mRNA or superactivation of the protein.
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PMID:Gene regulation during anaerobiosis in soya roots. 262 97

Plasma contains many enzymes that are probably derived from damaged cells. These enzymes are cleared at characteristic rates. We showed previously that in rats the rapid clearance of alcohol dehydrogenase, lactate dehydrogenase M4 and the mitochondrial and cytosolic isoenzymes of malate dehydrogenase is largely due to endocytosis by macrophages in liver, spleen and bone marrow. We now demonstrate that uptake of each of the enzymes by these tissues is in general decreased by simultaneous injection of a high dose of one of the other dehydrogenases or a high dose of adenylate kinase or creatine kinase. A similar dose of colloidal albumin did not significantly decrease uptake of the four dehydrogenases. Nor was uptake of colloidal albumin, apo-peroxidase from horseradish or multilamellar liposomes influenced by a high dose of mitochondrial malate dehydrogenase. These results indicate that the four dehydrogenases and the two kinases are specifically endocytosed via the same receptor. We suggest that this receptor contains a group, possibly a nucleotide, with affinity for the nucleotide-binding sites of the enzymes.
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PMID:Several dehydrogenases and kinases compete for endocytosis from plasma by rat tissues. 299 34

Transferrin accumulates within neurons of the developing nervous system of humans, sheep, pigs and chickens. To assess the relationship of this accumulation with the ontogeny of oxidative metabolism, we studied the immunocytochemical localization of transferrin (Tf) and the mitochondrial form of malate dehydrogenase (mMDH) in developing neural tissues by the peroxidase-antiperoxidase method. Rabbit anti-rat Tf was obtained commercially and gave a single band of reaction product (MW = 80 kd) on Western blots. Antibodies to porcine heart mMDH were elicited in a rabbit. Western blot analysis showed that this anti-porcine mMDH antibody reacted with the mMDH from porcine, rat or avian tissue but not with the cytosolic MDH from pigs. Tf was first detected in rat brain neurons at about the 18th embryonic day and reached a peak at about the 6th postnatal day. All neurons were immunoreactive with large neurons throughout the brain showing a strong reaction for Tf. From this time onward, the level in brain neurons gradually decreased until adulthood. However, Tf immunoreactivity still remained strongly evident in capillary endothelial cells. The localization of Tf within rat spinal cord neurons peaked as early as the 1st postnatal day and remained elevated to the 6th postnatal day. By contrast, reactivity for Tf within dorsal root ganglia neurons was intense as early as the 18th embryonic day and diminished only gradually. Mitochondrial MDH, a marker for oxidative metabolism, appeared to reach a peak after the crest of intraneuronal Tf had been observed. For example, brain and spinal cord MDH immunoreactivity increased with intense staining in the cell bodies and fibers of neurons from the 6th to the 13th postnatal day; immunoreactivity gradually diminished into adulthood. The gradient of reactivity was low in some areas of the brain but more intense in areas containing large neuronal cell bodies such as the red nucleus. This occurred after the peak of intraneuronal Tf at day 6 and suggested a precursor-product relationship. By contrast, immunoreactivity for neuron-specific enolase, a glycolytic enzyme, showed a developmental pattern that differed from either Tf or MDH in that reactivity appeared later in development and was less intense. These data suggest that as cerebral metabolic rates begin to increase as early as 5-6 days after birth in the rat, an increase in mMDH occurs coincident with the onset of oxidative metabolism. Furthermore, this rise in intraneuronal mMDH follows the peak of intraneuronal Tf and suggests that Tf supplies the iron required for the synthesis of other mitochondrial ferroproteins.
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PMID:Immunocytochemical localization of transferrin and mitochondrial malate dehydrogenase in the developing nervous system of the rat. 319 58

Ferguson plots demonstrated that corresponding malate dehydrogenase (MDH) isozymes of Durrant's L and S flax genotrophs differ in apparent molecular weight (MW) and also in net negative charge. The MW differences explain heritable differences in electrophoretic relative mobility (Rm) between corresponding L and S isozymes. The MW for each MDH isozyme was higher for L than for S and resulted in a slower Rm for L. The net negative charge for each isozyme was higher for L than for S. MDH isozymes also differ in MW within L and S. MW was lower for isozymes in leaves from the bottom of the stem than in leaves from the top of the stem, particularly in L. Integration of information on the MDH isozyme system in the flax genotrophs and information on the peroxidase system suggests the possibility that common modifier loci may control Rm in both enzymes.
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PMID:Malate dehydrogenase isozymes in flax genotroph leaves: differences in apparent molecular weight and charge between and within L and S. 340 77

The subcellular location and some properties of the rat kidney 25-hydroxyvitamin D3-1 alpha-hydroxylase are described. Enzyme activity can be measured as previously discussed (Tanaka, Y., and DeLuca, H.F. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 196-199) using saturating substrate (25-hydroxyvitamin D3) concentrations. The reaction is linear with time for up to 30 min at a substrate concentration of 80 microM and 9-11 mg/ml mitochondrial protein. The enzyme, located in the mitochondria, requires molecular oxygen and a source of NADPH. Succinate supplies NADPH for 1 alpha-hydroxylation through reversal of electron transport and transhydrogenation as shown by inhibition with antimycin A and dinitrophenol. Malate supplies NADPH for the reaction via the mitochondrial malic enzyme or malate dehydrogenase and transhydrogenase as indicated by the lack of inhibition by antimycin A but inhibition with dinitrophenol. Metyrapone and carbon monoxide both inhibit 1 alpha-hydroxylation indicating the involvement of cytochrome P-450. Diphenyl-p-phenylenediamine, a lipid peroxidase inhibitor, has no effect on 1 alpha-hydroxylation.
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PMID:Subcellular location and properties of rat renal 25-hydroxyvitamin D3-1 alpha-hydroxylase. 404 67


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