Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The distribution of enzymes, viz., alkaline phosphatase, acid phosphatase, adenosine monophosphatase and adenosine triphosphatase was studied by histochemical methods in the accessory respiratory organs of two fresh-water fishes (Clarius batrachus and Heteropneustes fossilis). Enzymes have been used as markers to differentiate between functional and non-functional cells of the dendritic organ of Clarius and of the air chamber of Heteropneustes. The variations in the enzyme activities have been correlated with the functional capacity of each respiratory organ. It is attempted to understand the physiological role of these enzymes in the process of aerial breathing.
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PMID:Phosphatases in the accessory respiratory organs of two fresh-water fishes. 20 22

Ultrastructural distribution of acid phosphatase and adenosine triphosphatase was studied in the receptor elements of HERBST and GRANDRY sensory corpuscles. Acid phosphatase activity was established in the elements of smooth and rough endoplasmic reticulum of perineural capsule cells, as well as in the secondary lysosomes of all cell types. Particular interest was paid on the activity of myelin-like dense bodies and some clear core vesicles belonging to the axoplasm of receptor nerve fibres. Adenosine triphosphatase activity was established on the membranes of receptor structures and pinocytotic vesicles. More deposits of electron dense material were localized on the axolemma of the non-myelinated portions of the receptor nerve fibres. The functional significance and importance of the both enzymes in the receptor structures was discussed.
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PMID:Cytochemical localization of acid phosphatase and adenosine triphosphatase in some avian mechanoreceptors. 21 19

Comprehensive investigations were carried out for establishing the biological and nutritional value of low erucic-acid rapeseed oil from a variety of rape called Janpol selected in Poland. The pathophysiological effects of Janpol rapeseed oil were observed after giving it as the only source of fat in the diet or added in different proportions to other edible fats. In all cases the total amount of fat in the diet was 20 p. 100 kcal. The investigations were carried out on 78 young male Wistar rats aged 25 days at the beginning of the experiment. The rats were divided into 7 groups and they were given diets containing: 1) soybean oil; 2) mixed fats; 3) rapeseed oil of high erucic-acid content; 4) mixed fats containing 25 p. 100 of Janpol rapeseed oil; 5) mixed fats with 50 p. 100 of Janpol rapeseed oil; 6) mixed fats with 75 p. 100 of Janpol rapeseed oil; 7) Janpol rapeseed oil only. The experiment lasted 3 months. After its completion the rats were decapitated after 18 hours of starvation. The investigation s included : determination of weight gain, determination of the weight of selected organs (liver-lungs, heart, kidneys, testes, spleen), determination of alkaline phosphatase and pseudocholinesterase activity in the serum, determination of triglycerides and cholesterol in the serum, tests for adrenocortical function, histo-chemical investigations of the liver (alkaline and acid phosphatase, adenosine triphosphatase, fatty infiltration of the liver), macroscopic and microscopic anatomopathological examinations. The authors found the Janpol rapeseed oil caused less pronounced changes in the determined indices of the biological and nutritional evaluation as compared with high-erucic-acid rapeseed oil. Janpol repeseed oil given to experimental animals mixed with other fats in proportions of 25 p. 100 and 50 p. 100 of all fats in the diet, that is 5 p. 100 and 10 p. 100 kcal in the diet derived from Janpol oil gave in most determinations of the investigated parameters results very similar to those observed in animals receiving soybean oil. The results of these investigations show that Janpol rapesed oil can be used for nutrition of man in amounts not exceeding 10 p. 100 of the total caloric content of food.
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PMID:[Nutritional and biological experiences on low-erucic acid rapeseed oil "Janpol". Studies on rats after ingestion of "Janpol" oil and other edible fats]. 22 Sep

In order to establish whether a specific adenosine triphosphatase is present in yeast cell wall, hydrolysis rates for p-nitrophenylphosphate (acid phosphatase activity) and for ATP (ATPase activity) were compared under various conditions. Rate determinations were made with both, intact cells and with preparations containing secreted enzymes from protoplasts. Acid phosphatase and ATPase activities had the same pH profile and were susceptible in the same way to the repression by orthophosphate and to the inhibition by 2-deoxyglucose. The Lineweaver-Burk plot shows biphasic kinetic behaviour for the hydrolysis of either p-nitrophenylphosphate or ATP. This suggests the existence of two enzymes with different affinities for the substrates, or one enzyme with at least two active sites. The two activities differ in thermostability and only one activity could be completely abolished by heat treatment. The thermostable enzyme activity had K-m values of 0.475 mM for p-nitrophenylphosphate, and 0.040 mM for ATP. ATP behaved as a partially competitive inhibitor of p-nitrophenylphosphate hydrolysis. Substrate competition studies showed that only a non-specific acid phosphatase is responsible for the hydrolysis of ATP.
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PMID:Acid phosphatase and adenosine triphosphatase activities in the cell wall of baker's yeast. 23 59

Dual localization of acid phosphatase in lysosomal and extralysosomal sites of the tubule epithelial cells of normal mouse kidney was observed at the light and electron microscope level using a modified Gomori lead-salt method with p-nitrophenylphosphate (pNPP) as substrate. Based on previous biochemical and cytochemical findings, we developed optimal conditions for the enzyme activity in extralysosomal sites. The conditions used for the light microscopic level consisted of 1.5 mM PNPP, 2.0 MM Pb(NO3)2 and 0.05 M acetate buffer (pH 5.8). Those for the electron microscopic study required 3.0 mM PNPP, 3.6 MM Pb(NO3)2 and 0.1 M acetate buffer (pH 5.8). This modified lead-salt technique was highly specific and provided a suitable method for the demonstration of nonlysosomal as well as lysosomal sites of acid phosphatase activity in the tubule epithelial cells of normal mouse kidney. As expected, the enzyme activity appeared in the lysosomes, but the prominent reaction in the brush border, the rough endoplasmic reticulum and basal infolding plasma membranes was not anticipated. We were able to demonstrate in situ organelle precursors of microsomal acid phosphatase such as endoplasmic reticulum, plasma membrane and basal infolding membranes showing the same substrate preference, which had been observed previously in biochemical studies in our laboratory. Since the possible participation of alkaline phosphatases, K+-pNPPase or Na+-K+-adenosine triphosphatase was ruled out by use of appropriate inhibitors, the enzyme-reactive sites can be interpreted as reflecting nonspecific acid phosphatase.
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PMID:Demonstration of lysosomal and extralysosomal sites for acid phosphatase in mouse kidney tubule cells with p-nitrophenylphosphate lead-salt technique. 23 53

56 human liver biopsy specimens with insignificant or no histological changes, but with abnormally strong canalicular alkaline phosphatase activity, were studied histochemically for other enzyme changes. In comparison with normal specimens, more extensive and increased canalicular activity of gamma-glutamyl transferase, and increase of canalicular leucine aminopeptidase, was found, while the sinusoidal activity of the latter enzyme was decreased. Staining for adenosine triphosphatase regularly desclosed the normal pattern of sinusoidal and canalicular activity. The lysosomal enzymes, acid phosphatase and beta-glucuronidase, stained more intensely than ordinarily, while the reactions for enzymes present in the cytosol (lactic dehydrogenase), in the mitochondria (succinic dehydrogenase, imonoamine oxidase) and in the endoplasmic reticulum (glucose-6-phosphatase) were normal.
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PMID:On histochemical enzyme changes in association with canalicular activity of alkaline phosphatase in human liver. 24 Dec 3

With histochemical methods the distribution of some enzymes and metabolic substances in the epidermal peelings of Phaseolus mungo, Lathyrus sativus, and Opuntia elatior under light and dark conditions is examined. Dehydrogenases oxidases, transferases and hydrolases were studied. Fluctuations in the activity of hydrolases, especially, acid phosphatase, lipase, glucose-6-phosphatase, adenosine triphosphatase, dehydrogenases and transferases were observed during light and dark conditions. The role of such fluctuations in relation to stomatal regulation is discussed. Based on the present studies the following is suggested; stomatal opening and closing is related to structural and metabolic changes, and these changes are brought about by sugar gradients in the guard cells; light is enhancing the synthesis of sugars and some hormones, and besides this it stimulates membrane bound adenyl cyclase and release of cyclic AMP which affects the permeability; subsidiary cells actively participate in the stomatal physiology. Lysosomal hydrolytic enzymes like acid phosphatase are actively involved in catabolic phase of normal guard cells metabolism and regulate the osmotic pressure of the guard cells.
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PMID:Histochemical studies in stomatal apparatus of Phaseolus mungo Linn, Lathyrus sativus Linn and Opuntia elatior Mill. 59 72

This study demonstrates the changes of concentration and elimination of calcium, phosphate and zinc, as well as alteration of serum alkaline phosphatase and acid phosphatase especially in patients with severe brain injuries in connection with bone fractures. Because the study has not been completed, the presently acquired results should only demonstrate possible development of the examined parameters. To find out the pathogenesis of overgrowing callus in brain-injured patients, further examinations are being carried out to find the histochemical activities of alkaline and acid phosphatase, lactate dehydrogenase, adenosine triphosphatase and acetylcholine esterase.
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PMID:[Special aspects of fracture healing in cranio-cerebral injuries]. 72 99

Organ cultures of malignant tumours were histochemically and electronmicroscopically investigated. There was established that follows enzymes show a little activity in cultured tumour cells after 24 and 48 h: succinate dehydrogenase, alkaline phosphatase, adenosine triphosphatase, and nonspecific esterase, whereas NADH-diophorase, lactate dehydrogenase, and acid phosphatase show an essentially higher activity after termination of the cultivation. However, in comparison with the primare tissue, the activities of the last mentioned enzymes are clearly decreased in cultured tumour cells after termination of the cultivation. No changes of cell structures have electronmicroscopically been observed on these cultures of malignant tumours.
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PMID:[Histochemical and ultrastructural investigations on organ culture of malignant tumors (author's transl)]. 81 69

The dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86


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