Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using histochemical techniques, changes in the localization of different reserve substances (e.g. pectic compounds, starch, polysaccharides, proteins, nucleic acids, ascorbic acid) and enzymes (Acid phosphatase, alkaline phosphatase, ATP-ase, 5-nucleotidase, esterase, phosphorylase, succinate dehydrogenase, cytochrome oxidase and lipase) have been studied in the young and fertilized ovules of Zephyranthes sp. and Lagenaria sp. etc. Extensive changes in the enzyme activity and reserve substances are demonstrated during megasporogenesis and megagametogenesis and most of the substances exhibited interesting distributional pattern. Similarly, all the enzymes investigated have specific locale of distribution in the tissues which displayed differentiation of embryo sac. The earlier changes observed are in the megaspore which contained many reserve substances (starch; nucleic acids; ascorbic acid; proteins) and enzymes (peroxidase, succinate dehydrogenase, acid phosphatase, alkaline phosphatase and ATP-ase). In the matured embryo sac different cells have differential localization of the substances. Based on histochemical studies, distinct differences are made out between egg and synergids; egg and central cell. In general antipodals have maximum accumulation of physiologically active substances and intense activity of different enzymes. Nucellus cells also stored diverse substances and enzymes especially towards the chalazal end. Pollination stimulated accumulation of several reserve substances and enzymes in the tip of nucellus beak, micropylar zone and these included starch, peroxidase, phosphorylase succinate dehydrogenase, cytochrome oxidase etc.
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PMID:Physiology of sexual reproduction. I. A histochemical study of the embryo sac development in Zephyranthes rosea and Lagenaria vulgaris. 81 Oct 56

For the purpose of describing early chondrogenic metabolic and structural events, measurements were made of oxidative and other enzymatic activities at various stages in the morphologic development of chondrocytes over a period of 18 to 20 days in continuous cell culture. Comparisons were also made between cells grown in 20% O2 and in 35% O2. These cultures exhibited rapid confluence (within 24 hours), early development of cartilaginous nodules by Day 2 to 3 and metachromatic staining of the chondrocyte matrix by Day 3 to 4. Under 35% O2, cell sheets were thicker and there was increased pleomorphism of chondrocyte and fibroblast cell types, with a relative increase of fibroblast components and reduction in chondroblasts and chondrocyte aggregates. Using the von Kossa staining procedure, calcium salt deposition was observed by Day 9. There was no apparent difference in mineralization of cultures grown under the low and high O2 tensions. Under normoxic conditions cytochrome oxidase and malate dehydrogenase (MDH) activities increased rapidly for the first three to four days and then remained essentially constant. Lactate dehydrogenase (LDH) activity increased continuously over the life of the culture. Acid phosphatase increased rapidly until about Day 13 after which it remained constant, whereas alkaline phosphatase showed a bimodal activity profile. Under hyperoxic conditions, cytochrome oxidase, MDH and alkaline phosphatase activity were significantly inhibited. LDH and acid phosphatase activities were markedly inhibited initially but with time showed a degree of recovery.
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PMID:Development of chick limb bud chondrocytes in cell culture: morphologic and oxidative metabolic observations. 701 57

Chronic administration of Senna occidentalis seeds induces an experimental toxic myopathy characterized by skeletal muscle fibers atrophy, decrease in histochemical activity of cytochrome oxidase, and increase of the acid phosphatase activity in muscle fibres at the light microscopic level. The mechanisms that lead to the increase of this lysosomal enzyme activity are not known and could be related to other biochemical disturbs than the mitochondrial function impairment. The main aim of the present study is to localize the acid phosphatase activity using a cytochemical method at transmission electron microscopy level and to quantify cathepsin D in muscle of rats chronically intoxicated with Senna occidentalis seeds by immunoblotting. Acid phosphatase was observed in lysosomes and over profiles of some organelles apparently not involved by lysosomal membrane. In addition immunoblotting demonstrated a decrease in the content of the precursor and of the mature form of cathepsin D in samples of muscles and liver of intoxicated animals. We concluded that there is a selective increase in acid phosphatase activity in muscle--and maybe in other tissues--of animals intoxicated with Senna occidentalis, that can be related to the skeletal muscle atrophy and the intense decrease in weight gain of these animals. Further studies should be performed to establish the mechanisms of selectivity in increase of lysosomal enzymes in different situations and pathological states.
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PMID:The lysosomal enzymes acid phosphatase and cathepsin D in rats intoxicated with Senna occidentalis seeds. 1045 11

Ultrastructural cytochemical techniques were used for the localization of phosphatases and oxidases in spermatid and spermatozoon of the phytophagous bugs Acrosternum aseadum and Nezara viridula (Hemiptera: Pentatomidae). Acid phosphatase was found mainly in the trans most portion of the Golgi complex, and in the acrosome of spermatozoon. Glucose-6-phosphatase was located in the endoplasmic reticulum, trans portion of the Golgi complex and in the acrosome of spermatids. The axoneme showed activity of acid phosphatase, glucose-6-phosphatase and thiamine pyrophosphatase. This observation supports the idea that various phosphates may play some role in spermatid differentiation. Indeed, the presence of cytochrome oxidase activity was only shown in the mitochondrial cristae of early spermatids, suggesting also the participation of this enzyme during spermatid differentiation of this insect.
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PMID:Ultrastructural localization of enzymatic activity during spermiogenesis in two phytophagous bugs (Hemiptera: Pentatomidae). 1862 62