Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

The histochemistry of the neural cells was studied in the submandibular ganglia of 5 Callithrix jacchus (3 males and 2 females) and 4 Callithrix penicillata (2 males and 2 females). These cells contain neutral mucopolysaccharides, nucleoproteins and lipidic materia, but are apparently devoid of glycogen. It is impossible to demonstrate in them any reactivity for UDPG-GT, phosphorylases, ATPase at pH 6.3, leucine aminopeptidase and alanyl aminopeptidas. The reaction for the other searched enzymes was as follows: weak (F-1,6-P Ald and cytochrome oxidase), weak to moderate (ADH, 6-P-GDH, ICDH, SDH, MDH, alpha-GPDH and beta-OHBDH), moderate (G-6-PDH, F-1,6-PA, LDH and GDH), moderate to strong (ATPase at pH 7.4, nonspecific esterase and acid phosphatase) and strong (G-6-PA, NADH2,-TR, NADPH2-TR, ATPase at pH 8.5 and 9.4 and alkaline phosphatase).
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PMID:Histochemical studies on the submandibular ganglia of marmosets (Callithrix jacchus and Callithrix penecillata). 14 13

The influence of the herbicide balagrin on the maternal organism and fetus was experimentally studied on 60 pregnant albino rats of Wistar line. The preparation was given orally throughout the entire gestation period in daily doses of 1/1o - 110 mg/kg, 1/20 - 55 mg/kg and 1/50 - 22 mg/kg of LD50 - 1100 mg/kg. The detoxifying function was studied by the duration of hexabarbital sleep, the excretory function - by the cholic acid content in the bile, and the enzymatic function - by the dehydrogenase activities: LDH, MDH, LDH, GL-6-PDH in the liver of pregnant animals and the fetus, Marked toxic effect on the maternal and fetal organism was demonstrable at all balagrin application levels by the liver function disturbances.
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PMID:[General toxicity and specific action of the herbicide balagrin]. 46 5

Specific activities of enzymes in bovine hearts were measured. The enzyme activity ratios between the conduction system and the myocardium were 1.9 for G-6-PDH, 1.2 for PFK, 0.5 for total phosphorylase and LDH, 0.4 for GOT and MDH, 0.3 for SDH, 0.2 for Aldolase and CPK, and 0.1 for alpha GPDH. Approximate values for relative volume of Purkinje cells, nerve fibers and connective tissues in the conduction system were 30%, 8%, and 62%, respectively. It is concluded that activities of enzymes serving for anaerobic glycolysis in Purkinje cells are almost the same or slightly higher than those in the myocardium, and activity of enzyme for pentose shunt in the conductive tissue is higher than that in the myocardium.
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PMID:A comparison of enzyme activity for energy production in the myocardium and conduction system. 50 32

The structure and histochemistry of the palmar and plantar skin were studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). In this skin there exist well-developed epidermal ridges, to which are attached one or two ducts of sweat glands. A thick stratum corneum can be seen in the epidermis, while a distinct stratum lucidum cannot be isolated from the other layers. The stratum granulosum is constituted by one or three layers of cells containing keratohyalin granules. Melanin granulations are mainly concentrated in the basal cells of the epidermal ridges. Dendritic melanocytes and amelanotic melanocytes containing alkaline phosphatase are found among the epidermal cells. Glycogen, UDPG-GT and phosphorylases are mainly present in the middle and lower Malpighian cells of the epidermal ridges. Alkaline phosphatase, ATPase, alanyl amino-peptidase and leucine aminopeptidase were absent in the epidermal cells. SDH, cytochrome oxidase, MAO and a certain number of NAD-dependent dehydrogenases (LDH, ADH, MDH, alpha-GPDH, beta-OHBDH and GDH) showed a stronger reactivity in the basal cells and Malpighian layer. The NADP-dependent enzymes (G-6-PDH, 6-PGDH, cis-aconistase and ICDH) were more reactive in the upper Malpighian layer and stratum granulosum. The stratum corneum showed some acid phosphatase and nonspecific esterase reactivity. The collagenous fibers intertwined with a small number of very thin elastic ones and a larger amount of reticular fibers run almost parallel to the epidermal ridges in the papillary body. In the reticular dermis some fibers are disposed transversely to the epidermal ridges. Meissner corpuscles reactive to butyrylcholinesterase, acetylcholinesterase, nonspecific esterase and G-6-PA are disposed at regular intervals and frequently at each side of the epidermal ridges. Pacinian corpuscles were found only in the hypodermis. The eccrine sweat glands contain glycogen, UDPG-GT and phosphorylase in their secretory, ductal and myoepithelial cells. The secretory part shows a uniform reactivity for every dehydrogenase because it contains only one type of cells (clear cells). The intraepidermal segment of the ducts shows a stronger reactivity to nonspecific esterase and NADP-dependent dehydrogenases than the epithelial cells around it.
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PMID:The skin of the palms and soles of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 86

Changes in LDH, SDH, MDH and G-6-PDH activity in the liver of white male rats are studied within 2, 4, 8, 15, 30, 60 and 90 days of treatment with 1/10 and 1/50 LD50 and after 15 days recovery period following the 90-day-long treatment. The animals are divided up into three groups as follows: group one--treated with 1/10 LD50, group two--with 1/50 LD50, and a control group treated with vegetable oil solvent at the respective days. The findings show that changes in enzyme activity are comparatively one-way in terms of duration of the treatment. In the early days of the experiment, a reliable increase is noted followed by a normalization of the values and reliable reduction. At ninety days, and after the recovery period is over, the activities of all five enzymes do not differ from those in the control groups. The most clearly outlined changes are recorded in SDH, and the slightest--in MDH. The analysis of the picture obtained shows that in all instances it is a matter of reversible changes.
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PMID:[Changes in liver dehydrogenase activity in rats with Unden poisoning]. 103 22

The content of the Krebs cycle substrates and activity of dehydrogenases corresponding to them were studied in the brain and myocardium tissues of the non-linear male rats adapted to acute hypoxia under conditions of the altered gas medium. The content of malate and succinic acid was studied in the liver and skeletal muscles only. In the brain the total activity of malate dehydrogenase (MDH, EC 1.1.1.37, 1.1.1.39) alpha-ketoglutarate dehydrogenase (KDH, EC 1.2.4.2) pyruvate dehydrogenase (PDH, EC 1.2.4.1) and isocitrate dehydrogenase (ICDH, EC 1.1.1.41-42) is shown to be decreased and kept to be lowered in all the periods of the study. No essential shifts in the activity of these dehydrogenases were found in the myocardium. The activity of succinate dehydrogenase (SDH, EC 1.3.99.1) in both tissues lowers 48 h after the effect of the mentioned factors. Simultaneously the greatest changes in the level of the substrates were observed in the myocardium, in the brain they were less developed. In the liver the content of malate increases without pronounced changes in the amount of succinic acid and in the skeletal muscles the level of malate and succinic acid lowers.
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PMID:[Krebs cycle in tissue of rats subjected to combined effect of hypercapnia, hypoxia and cooling]. 121 51

Since glycogen overloading is one of the outstanding features of the diabetic liver, a series of investigations were undertaken to find an enzymatic explanation of this feature. Three groups of patients were studied: non diabetics submitted to liver biopsy during surgery (group A); non diabetics submitted to percutaneous liver biopsy (group B). In both these groups G-6-PDH, PK and MDH were assayed, all these being adaptive enzymes of intermediate metabolism. Results were expressed as muU/100 mg proteins. The significant finding of the comparison of these two groups was the low concentration of these enzymes in surgical biopsies. The depression was such that for G-6-PDH the concentration was more than 10 times less in surgical specimens as compared to percutaneous ones, whereas for PK it was almost 10 times less. In view of these findings no further surgically obtained biopsy material was used in this study. The third group (C) included insulin-dependent diabetics in good metabolic control from whom percutaneous liver biopsies were obtained for the assay of the same enzymes as above and in order to compare the results with those of group B. All three enzymes were diminished in diabetics, the difference being statistically significant for G-6-PDH and PK, not for MDH in view of the wide dispersion of the values found. Comparison and analysis of these results lead to the conclusion that in view of the low concentration of these enzymes in diabetics, glucose utilization in the liver cell must be presumed to be increased via other metabolic pathways.
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PMID:The liver in human diabetes. Concentration of some induced enzymes. 123 63

Some histochemical changes in adult C. sinensis collected from rats infected artificially and treated with pyquiton were observed. 1 h after administration the glycogen content showed a slight decrease which became prominent 24h later and almost disappeared at 48h post-medication. There was an increase in protein content in the parenchymal tissues of worms 1h after treatment, especially in the reproductive organ 24h after treatment. RNA content was decreased 1h post administration and continued decreasing gradually so that very little could be seen 48h later. An increase in the activities of SDH, MDH and Ca-ATPase was seen at the beginning and became marked 24h after medication, while that for G-6-PDH was detected 48h after drug administration. No obvious changes in DNA, lipid, AKP, ACP and phenolase were detected within 1-48h after treatment.
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PMID:[Histochemical changes in Clonorchis sinensis after pyquiton treatment]. 169 37

Aldrin toxicity was studied in the brain, liver and muscle of Rana hexadactyla. It was observed that sublethal concentration of aldrin inhibited the activities of SDH, MDH and ICDH while it elevated the activities of LDH and G-6-PDH. The increase and the decrease was progressive with the exposure period. The changes were attributed to the induced toxic effects such as oxygen distress, energy crisis and microstructural changes.
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PMID:Aldrin toxicity on amphibian neuronal, hepatic and muscular tissue oxidative enzymes. 228 77


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