Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.6.99.3 (diaphorase)
5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A morphological and histochemical study has been made of the primordial and early growing oocytes in the ovaries of crow (Corvus splendens) and common myna (Acridotheres tristis). The primordial oocytes in the myna ovary are loosely arranged in groups or nests, whereas in crow they form compact nests surrounded by highly vascularized connective tissue bands or lie in layers beneath the surface epithelium. The primordial oocytes in both the species are surrounded by flat granulosa cells whose number, shape, and cytochemical properties change with the initiation of growth. The oocyte nucleus shows a single basophilic nucleolus and thick diplotene chromosomes. With the initiation of growth, the number of nucleoli increases; simultaneously the chromosomes attain lampbrush configuration. Crescent-shaped Balbiani's vitelline body consists of ribonucleoproteins, lipoproteins, and phospholipids. The amount of these substances increases with the oocyte growth. The nature of proteins and lipids in the ooplasm and follicular epithelium also changes with the oocyte growth. Some randomly distributed protein bodies are also present in the ooplasm of primordial follicles. They disappear with the initiation of oocyte growth. The enzyme activities of acid phosphatase, NADP-diaphorase and NAD-diaphorase, also increase in the Balbiani's vitelline body with the oocyte growth. Alkaline phosphatase and delta 5-3 beta-HSDH activities are not seen. The possible functional significance of these morphological and histochemical changes has been discussed in relation to the initiation of growth in quiescent oocytes.
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PMID:Morphological and histochemical observations on the primordial and early growing oocytes of crow (Corvus splendens) and myna (Acridotheres tristis). 47 89

In vitro alterations induced by a 10 micrograms/ml and 50 micrograms/ml dose each of thiophenate and fenbendazole on the absorptive surfaces of Haemonchus contortus (Nematoda: Trichostrongylidae) were studied. The most significant changes were induced in the gut epithelium. Alkaline phosphatase and adenosine triphosphatase activities were decreased, succinic dehydrogenase activity was increased, while acid phosphatase and glucose-6-phosphatase were completely lost from the intestinal epithelium after treatment with either of the drugs. A stimulatory effect of these two anthelmintics was observe on lactic dehydrogenase and reduced nicotinamide adenine dinucleotide diaphorase distribution. Thiophenate caused an increase in the activities of glutamate dehydrogenase (GDH), glucose-6-phosphate dehydrogenase (G-6-PD) and nonspecific esterases and a decrease in reduced nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-D) activity. Fenbendazole treatment led to the inhibition of GDH, while G-6-PD, NADPH-D, cytochrome oxidase, monoamine oxidase and nonspecific esterase activity remained unaltered in the epithelium.
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PMID:Histoenzymic effects of thiophenate and fenbendazole on the absorptive surfaces of Haemonchus contortus. 133 82

A sensitive enzyme immunoassay was developed for human angiotensin converting enzyme. Monoclonal antibodies specific for two unique converting enzyme epitopes were utilized to develop a two-site sandwich enzyme immunoassay. Alkaline phosphatase conjugated to the detecting antibody hydrolyzes nicotinamide adenine dinucleotide phosphate (NADP) to NAD. Subsequently, NAD is cycled between its reduced and oxidized forms by an alcohol dehydrogenase/diaphorase catalyzed redox cycle. Each cycle converts iodonitrotetrazolium violet to a highly colored formazan which is quantitated. With this assay, as little as 94 pg/ml of native converting enzyme is detectable without interference from either therapeutic or endogenous converting enzyme inhibitors.
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PMID:A sensitive two-site sandwich enzyme immunoassay for human angiotensin converting enzyme utilizing monoclonal antibodies. 169 77

Methods of disaggregation of human placental tissue were assessed with the aim of maximising the yield of cytotrophoblast cells and minimising contamination with other cell types. Brief exposure to crude trypsin was found to be the best way to balance yield of trophoblast cells against contamination by cells of the villous core. Much higher yields of all cell types could be obtained by digestion with other enzymes. Staining for NADH diaphorase activity coupled with general morphology was found to be a reasonably specific, rapid and simple method of distinguishing cytotrophoblast cells in disaggregated mixtures. Alkaline phosphatase activity was an unreliable marker of trophoblast tissue in early placentas, and of the putative cytotrophoblast cells in mixtures of disaggregated cells. Cultures of cells obtained from term placentas were fairly homogeneous, whereas placentas of 6-12 weeks gestation gave heterogeneous cell cultures which became overgrown with fibroblasts.
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PMID:Human placental cytotrophoblast cells: identification and culture. 267 72

Alkaline phosphatase was released from protoplasts of the yeast Saccharomyces cerevisiae without cell lysis not only by phosphatidylinositol (PI)-specific phospholipase C but also by phosphatidylcholine (PC)-hydrolyzing phospholipase C. Activities of mitochondrial enzymes such as succinate dehydrogenase, antimycin-sensitive NADH-cytochrome c reductase, and oligomycin-sensitive ATPase were decreased by the action of PC-hydrolyzing phospholipase C. Hydrolysis of microsomal PC or PI did not cause any decrease in the activities of NADPH-cytochrome c reductase and antimycin-insensitive NADPH-cytochrome c reductase. In the requirement of phospholipids, the properties of yeast mitochondrial enzymes were very close to those of mammalian mitochondrial enzymes, whereas those of yeast microsomal enzymes were completely different from those of mammalian microsomal enzymes.
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PMID:Effects of phospholipases C on membrane-bound enzymes of yeast. 296 99

Osteogenesis of the body of the mandible in embryonic and neonatal rats was studied histologically and by histochemistry to determine the role of Meckel's cartilage in bone formation. Meckel's cartilage showed intense activity of lactate dehydrogenase and NADH2-diaphorase and weak activity of acid phosphatase, indicating a functioning citric acid cycle, pentose phosphate shunt and a capacity for anaerobic metabolism. The activity of these enzymes declined after hypertrophy of Meckel's cartilage. Alkaline phosphatase was the major enzyme of mineralising mandibular osteoid and was present in the osteoblasts and osteoprogenitor cells but not in Meckel's cartilage. After the differentiation of Meckel's cartilage and intramembranous bone, Meckel's cartilage supported mandibular bone formation by endochondral ossification in the anterior part of the mandible.
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PMID:Enzyme histochemical analysis of Meckel's cartilage. 325 49

The effects of irradiation on various tissues have been studied extensively. Nonetheless, the metabolism in growing bones has not been evaluated in a systematic way after moderate doses of irradiation. It was found that scattered radiation, that reaches the oral region during radiotherapy of malignancies outside the oral region, causes absorbed doses within the range of 0.2-20 Gy, while absorbed doses from radiography in orthodontics were only 30-40 mGy. Bone formation in the metaphyseal area of rat tibia in vivo after irradiation with 0.5-8 Gy was determined by a tetracycline labelling method. Five and 8 Gy induced a significant growth retardation. This was detectable already after 36 hours and was maximal 7-14 days after irradiation. Between 14 and 30 days following irradiation growth was normalized. Alkaline phosphatase (ALP) activity in bone was evaluated biochemically and decreased one day after irradiation with 0.5-8 Gy. This was followed by a gradual increase in ALP activity and a return to normal values 30 days after irradiation. Histochemical studies of the rat tibias included evaluation of ALP, acid phosphatase, NADH2-diaphorase and Glucose-6 phosphate dehydrogenase. A decrease in ALP activity one day after irradiation was observed with 5, 8, and 10 Gy. Acid phosphatase and the two oxidative enzymes were increased in activity during the entire 7-day experimental period, reflecting an altered metabolism. Normal activities of all the studied enzymes were observed 30 days after irradiation. Results from suture area and synchondrosis area as evaluated by histochemistry and a cephalometric radiographic method showed that early transient metabolic changes occurred in the craniofacial growth sites after irradiation with 5 and 8 Gy. The morphological changes observed in anatomical regions within the irradiated field (neurocranium) persisted in contrast to the changes in the viscerocranium that were normalized at the end of the experimental period. An in vitro system was used to examine the effects of irradiation on certain aspects of bone growth. Mice calvaria were irradiated in vitro with 2 or 10 Gy. A different response in suture and bone was found 3 hours to 4 days after irradiation. Bone was affected by 2 Gy, but not the suture. Thus, the suture seems to be an area with more radioresistant fibroblast-like cells than the cortical bone, which indicates a difference in radiosensitivity of the cells in these two growth sites. The conclusions from the present thesis are that irradiation with 2-10 Gy of bone both in organ culture and in experimental animals induces metabolic and morphologic changes which were detected early and were transient.
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PMID:Effects of irradiation on growing bones. 346 72

Microvillar vesicles have been isolated from rat placentae. The vesicles have been characterized with respect to their microscopic appearance, their capacity to accumulate amino acids, and their enzyme activities. Alkaline phosphatase activity in the vesicle fraction was threefold greater than in the homogenate, and cytochrome c reductase activity was decreased fourfold. The vesicles were used to characterize transferrin binding to the trophoblast membrane in vitro. Transferrin binding was specific (K alpha = 8 X 10(7) M-1), and could not be replaced by apotransferrin. Apotransferrin binding showed lower affinity than the diferric transferrin, and did not appear to saturate over the range 0 to 500 micrograms/ml.
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PMID:Transferrin binding by microvillar vesicles isolated from rat placenta. 609 Oct 92

Previous immunolabeling studies (Roman, L.M., and A.L. Hubbard, 1983, J. Cell Biol., 96:1548-1558; Roman, L.M., and A.L. Hubbard, 1984, J. Cell Biol., 98:1488-1496, companion paper) established leucine aminopeptidase (LAP) as a specific marker for the bile canalicular (BC) domain of the rat hepatocyte plasma membrane (PM). In this study, we have isolated membrane from a sonicated PM vesicle fraction using anti-LAP-coated Staphylococcus aureus cells as a solid-phase immunoadsorbent. The extent and specificity of the immunoadsorption were assessed by following the behavior of LAP (the BC marker) and 32P-labeled membrane phospholipids (a uniform membrane marker). The BC fraction obtained was significantly enriched in LAP (yield: greater than 70% of PM-LAP). Alkaline phosphatase, 5'-nucleotidase, and a 110,000-dalton glycoprotein, HA-4, were enriched in the BC fraction to the same extent as LAP (enzyme or antigen/LAP = 1.0). However, alkaline phosphodiesterase I was not enriched to the same degree (enzyme/LAP = 0.5). Contamination of this BC fraction by membrane derived from the sinusoidal domain and endoplasmic reticulum, as determined from the distribution of the asialoglycoprotein receptor and NADH cytochrome c reductase, respectively, was small (less than 13%).
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PMID:A domain-specific marker for the hepatocyte plasma membrane. III. Isolation of bile canalicular membrane by immunoadsorption. 637 Oct 22

The activities of alkaline phosphatase and reduced nicotinamide adenine dinucleotide (NADH) diaphorase in the principal cells of the guinea pig epididymis were studied histochemically. Alkaline phosphatase activity was absent from the principal cells but was present in the basement membrane of the epididymal epithelium. NADH diaphorase activity was distributed throughout the cytoplasm of the principal cells in each epididymal segment. There was a gradual increase in NADH diaphorase activity from segments 1 through 7. Possible functions of alkaline phosphatase and NADH diaphorase in the epididymis are discussed.
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PMID:Localization of alkaline phosphatase and NADH diaphorase in the principal cells of the guinea pig epididymis. 668 19


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