Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8NEX9 (reductase)
26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Modification in the enzymatic complement and lipogenic functions of rat liver endoplasmic reticulum (ER) were shown to occur during pneumococcal sepsis. Glucose-6-phosphatase, 5'nucleotidase, esterase, and NADPH cytochrome C reductase decreased in activity by as much as 50% with respect to controls. Hydroxymethylglutaryl-CoA and NADH cytochrome C reductases were increased 6-and 2-fold, respectively. Alkaline phosphatase and inosine-5'-diphosphatase did not differ with respect to fasted controls. The lipogenic capacity of the ER was shown to be enhanced. In vitro [14C]acetate incorporation into cholesterol and other lipids by hepatocytes isolated from infected rats was increased 2-to 10-fold. It is concluded that the flow of acetyl-CoA in liver cell of Streptococcus pneumoniae-infected rats is toward lipogenesis rather than ketogenesis.
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PMID:Effects of pneumococcal infection on rat liver microsomal enzymes and lipogenesis by isolated hepatocytes. 1 31

Scolices and brood capsules of healthy hydatid cysts from lungs of human patients were studied with histochemical and histoenzymatic methods. The subtegumental and flame cells were sepcially rich in glycogen, RNA and some dehydrogenases such as SDH, MDH, NADH-reductase and G-6-PDH. The rostellar zone or invaginated pole, an area of marked contractile movements, showed intense activity in ATP'ase and simple esterase. The so-called excretory pole shows strong activity in simple esterases, lipase, beta-HBH, alpha-GDH and NADPH-reductase. Lipids are also abundant in this zone implying the important role of this metabolic path in the development of the parasite. Intense activity in alkaline phosphatase was observed in cells associated to the calcereous corpuscles. The largest corpuscles were devoid of enzymatic activity. The enzyme could play some role in the calcification of the corpuscles. Wide enzymatic variations are described according to morphology being orthoscolices the most rich in enzyme activity. Accumulations of small cells surrounded by specialized cells on the germinal membrane are interpreted as the origin or "embryo" of brood capsules. Some enzymes detected in the wall of mature brood capsules depicted alternating types of cells. Some of them are positive for ATP'ase that may be related to active transport of substances across the brood capsule wall. The intenst ATP'ase activity at the stalks of scolices may be similarly interpreted. However, a miosine-like activity is a more feasible explanation since this area showed striking contractile movements in vivo.
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PMID:Histochemistry and histoenzymology of the hydatid cyst (Echinococcus granulosus Batsch, 1786). II. Scolices and brood capsules. 13 Jul 50

A complex bioptic examination of skeletal muscles as carried out in 280 excised samples has been subjected to a critical analysis. The examination suggested consists of histological and histochemical processing of native cryostat sections. Besides conventional staining methods the techniques recommended include the reaction for detection of myosin ATP-ase with and without acid preincubation, and reactions for NADH tertazolium reductase, acid phosphatase, nonspecific esterase, glycogen and lipids. Sections stained for ATP-ase are suitable for quantitative examinations such as assessing the diameters of muscle fibres.
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PMID:[Histochemical and quantitative methods in the biopsy examination of skeletal muscles]. 20 10

The maize root has two main proteinase and carboxypeptidase components. Proteinase I and carboxypeptidase I, which predominate in older plants, appear to have a serine group at their active sites and have been estimated to have molecular weights of approximately 54000 and 77000 respectively. Proteinase I, which has been purified up to 500-fold, degrades haemoglobin and azocasein with maximum activity at pH 4 and 9--10 respectively, while on maize root protein it gives most hydrolysis in the neutral pH range. The main portion of the nitrate-reductase-inactivating activity in the maize root extract is due to proteinase I. Carboxypeptidase I, like several other plant carboxypeptidases such as carboxypeptidase C which have now (IUB Recommendations 1978) been classified as serine carboxypeptidases (EC 3.4.16.1), has maximum activity around pH 5 and has esterase activity. A second group of proteases, proteinase II and carboxypeptidase II, separated from the above on carboxymethyl-cellulose, were shown to have different molecular weight properties and be equally sensitive to serine and thiol group inhibitors. Proteinase II degrades haemoglobin, but not azocasein and does not mediate nitrate reductase inactivation. Associated with this second group of proteases was a macromolecular component which inactivated nitrate reductase but, unlike the action of proteinase I, was not inhibited by phenylmethylsulphonyl fluoride or casein. It was inhibited by metal chelating agents which were without effect on nitrate reductase inactivation due to proteinase I.
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PMID:Isolation and characterisation of peptide hydrolases from the maize root. 39 8

In the paper we observed histochemically the distribution and activity of 16 enzymes in the normal rat gastric mucosa. The lysosomal enzymes were demonstrated by the method of semipermeable membranes (LOJDA 1972). At the proof of dehydrogenases aqueous and gel media were used. The parietal cells of the gastric mucosa contained a moderate activity of acid phosphatase, E-600 resistant esterase, and only a very slight activity of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase. The macrophages of the interstice contained a high activity of beta-glucruonidase, acid phosphatase, E-600 resistant esterase and a low activity of N-acetyl-beta-D-glucosaminidase. The chief cells of the rat gastric mucosa, in contrast to the human, did not contain nonspecific esterase and also in them acid phosphatase was mostly lacking. The alkaline phosphatase was found only in the endothelium of the capillaries of the gastric mucosa. The parietal cells contained high activities of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, NADH tetrazolium reductase, a lower activity of NADPH tetrazolium reductase, as well as other soluable dehydrogenases. At the examination of dehydrogenases using aqueous as well as gel media with PMS during optimal short incubation periods, we found more and less active forms of parietal cells. The different oxidoreductase capacity of parietal cells in normal rat gastric mucosa can point to their unequal-functional load at the production of hydrochloric acid. The findings obtained are compared with the findings in older papers concerning different experimental animals and with the distribution of enzymes in the human gastric mucosa.
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PMID:Histochemical localization of enzymes in the normal rat gastric mucosa using the technique of the semipermeable membranes and the other methods. 82 7

We have identified two distinct and consistent type I fiber subtypes in histochemically normal biopsies (vastus lateralis or biceps brachialis) from 12 healthy persons, both sexes, ages 15 to 42. The type I fibers were uniformly light with the regular ATPase (9.4) and uniformly dark with the acid-preincubated reverse ATPase reactions. However, the subtype IA fibers were stained darker than subtype IB fibers with the nicotinamide adenine nucleotide dehydrogenase-tetrazolium reductase, Oil red O, reduced nicotinamide adenine dinucleotide phosphate-tetrazolium reductase, nonspecific esterase, succinic-tetrazolium reductase, nicotinamide adenine dinucleotide-linked malic-tetrazolium reductase, and "nicotinamide adenine dinucleotide-linked lactic-tetrazolium reductase," and stained lighter with the phosphorylase, periodic acid-Schiff for glycogen, and menadione-mediated alpha-glycerophosphate-tetrazolium reductase reactions. The IB fibers were not as light (or as dark, depending on the stain) as any of the type II fibers. In one pathologic case, all the "hypotrophic type I muscle fibers with central nuclei" were subtype IB. In case of chronic infantile spinal atrophy the muscle showed some type-grouping and marked type I fiber predominance--the great majority of type I fibers were subtype IB, among which were islands (subtype-groups) of IA fibers. Subtyping of type I fibers may be informative in evaluating the pathologic process of certain human neuromuscular diseases.
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PMID:Distinct subtypes of type I fibers of human skeletal muscle. 117 13

Using the Hep G2 cell line as a model for the human hepatocyte the question was studied whether Hep G2-peroxisomes could be able to synthesize cholesterol. Hep G2 cell homogenates were applied to density gradient centrifugation on Nycodenz, resulting in good separation between the organelles. The different organelle fractions were characterized by assaying the following marker enzymes: catalase for peroxisomes, glutamate dehydrogenase for mitochondria and esterase for endoplasmic reticulum. Squalene synthase activity was not detectable in the peroxisomal fraction. Incubation of Hep G2 cells with U18666A, an inhibitor of the cholesterol synthesis at the site of oxidosqualene cyclase, together with heavy high density lipoprotein, which stimulates the efflux of cholesterol, led to a marked increase in the activity of squalene synthase as well as HMG-CoA reductase, whereas no significant effect on the marker enzymes was observed. Neither enzyme activity was detectable in the peroxisomal density gradient fraction, suggesting that in Hep G2-peroxisomes cholesterol synthesis from the water-soluble early intermediates of the pathway cannot take place. Both stimulated and non-stimulated cells gave rise to preparations where squalene synthase activity was comigrating with the reductase activity at the lower density side of the microsomal fraction; however, it was also present at the high density side of the microsomal peak, where reductase activity was not detected.
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PMID:Subcellular localization of squalene synthase in human hepatoma cell line Hep G2. 131 47

The authors studied distribution of alkaline and acid phosphatases, non specific esterase and NADH2 tetrazolium reductase in the dental pulp of children treated by fix orthodontic appliances. All the enzymes studied exhibited positive reaction, the activity, however, was lower than in the controls, except of the alkaline phosphatase. The results of the study demonstrated that the forces between 60-200 g cannot be evaluated as biologically favorable.
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PMID:[Histochemical observations on enzyme activity of the dental pulp following the orthodontic therapy]. 181 66

Tissue reactions toward biodegradable poly(L-lactic acid) implants were monitored by studying the activity pattern of seven enzymes as a function of time: alkaline phosphatase, acid phosphatase, alpha-naphthylacetyl esterase, beta-glucuronidase, ATP-ase, NADH-reductase, and lactate dehydrogenase. Cell types were identified by their specific enzyme patterns, their morphology and location. Special attention was paid to the enzyme patterns of macrophages, fibroblasts and polymorphonuclear granulocytes (PMNs), being involved in foreign body reactions or inflammatory responses. One day after implantation, an influx of neutrophilic and eosinophilic granulocytes was observed, coinciding with activity of alkaline phosphatase (PMN's) and beta-glucuronidase (eosinophils). From day 3 on, macrophages containing ATP-ase, acid phosphatase and esterase could be observed. From day 7 on, lactate dehydrogenase, the enzyme normally involved in the conversion of lactic acid, and its coenzyme NADH-reductase were observed in macrophages and fibroblasts. These two enzymes demonstrated more activity than expected on basis of wound-healing reactions upon implantation of a nonbiodegradable, inert biomaterial (as, e.g., Teflon). It is concluded that the biodegradable poly (L-lactic acid) used in these implantation studies is tissue compatible, and evokes a foreign body reaction with minor macrophage and giant cell activity, as observed during this 3-week implantation period. Most enzyme patterns were simply due to a wound-healing reaction. The slightly increased levels of LDH and NADH suggest the release of lactic acid from the implant, and thus confirms the biodegradable nature of this polymer.
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PMID:Enzymatic activity toward poly(L-lactic acid) implants. 232 25

Eighteen calves were orally inoculated with either 200,000 or 225,000 sporocysts of Sarcocystis cruzi. Eight goats were orally inoculated with 20,000 sporocysts of S capracanis. Calves and goats were euthanatized at various times after inoculation, and portions of their right and left biceps femoris, right and left longissimus dorsi, myocardium, and tongue were frozen at -150 C in precooled isopentane and stored at -70 C. Frozen sections of these muscles were stained with hematoxylin and eosin, modified Gomori's trichrome, nonspecific esterase, diphosphopyridine nucleotide tetrazolium reductase, and adenosinetriphosphatase at pH 10.4 and 4.6. Muscle from the same locations was fixed in 10% neutral buffered formalin, processed for paraffin embedding, sectioned, and stained with hematoxylin and eosin. Microscopic examination of both calf and goat tissue indicated that both type I and type II muscle fibers were equally infected and that infected myofibers showed no apparent damage other than displacement by sarcocysts. Occasionally, muscle fibers within the muscle spindles contained sarcocysts.
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PMID:Types of myofibers parasitized in experimentally induced infections with Sarcocystis cruzi and Sarcocystis capracanis. 242 18


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