Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human platelets separated from blood by six different methods have been compared for aggregability, adhesion to glass, adenine nucleotide content and release, and adenosine triphosphatase and cholinesterase activities. Methods of separation of platelets from blood included three differential centrifugation technics, gel filtration and two albumin density gradient methods. Platelets prepared by the different methods aggregated comparably except those separated by albumin density gradient technics which tended to be hyporeactive. Differences in adhesion to glass, adenine nucleotide content and release, and monitored enzyme activities of the various platelet preparations were noted in several cases but were not marked in general. Ultrastructural studies, reported elsewhere, revealed that platelets separated by the method of Mustard or by gel filtration were less altered morphologically than those separated by the other methods. Platelets separated from blood by gel filtration also appeared somewhat superior functionally to platelets separated by other methods.
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PMID:Comparison of certain functions of human platelets separated from blood by various means. 427 71

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

Human erythrocyte acetylcholinesterase and the plasma cholinesterase variants are not only inhibited by propranolol but have been found to show stereospecificity for its isomers. The erythrocyte enzyme has a greater affinity for the L-isomer than either the racemate or the D-isomer. In contrast the plasma cholinesterases have greater specificity for the D-isomer than the other isomer or racemate. The usual enzyme shows greater stereospecificity than the atypical enzyme and these findings present additional evidence that these enzyme variants differ in structure at the catalytic active site. Neither Na+ + K+ -ATPase nor Mg2+-ATPase show stereo-specificity for the isomers of propranolol although both enzymes are inhibited by the drug. The action of the drug on the four enzymes in blood samples obtained from patients having Huntington's disease was found to be identical to those observed on the enzymes in blood samples from healthy controls.
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PMID:Studies on the inhibition by propranolol of some human erythrocyte membrane enzymes and plasma cholinesterase. 612 Jul 72

1. Adult black ducks (Anas rubripes) were given freshwater or saltwater (1.5% NaCl) for 11 days and half of each group was also given an organophosphate (17 p.p.m. fenthion) in the diet on days 6-11. 2. After 11 days, ducks drinking saltwater had lost more weight and had higher plasma Na and uric acid concentrations and osmolalities than birds drinking freshwater. 3. Saltwater treatment stimulated the salt gland to increased weight and Na, K-ATPase activity. 4. Fenthion generally reduced plasma and brain cholinesterase activity and depressed cholinesterase and Na, K-ATPase activities in salt glands of birds drinking saltwater.
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PMID:Organophosphate inhibition of avian salt gland Na, K-ATPase activity. 612 65

Acetylcholinesterase (AChE) activity was measured in the presence of the specific inhibitor of pseudocholinesterase, iso-OMPA, in plasma from patients with amyotrophic lateral sclerosis (ALS), progressive muscular atrophy (PMA), neuromuscular disease controls, and normal controls. Both AChE and Na-K ATPase activities were measured in erythrocyte ghost membranes from ALS and normal controls. Activities of erythrocyte ghost AChE and Na-K ATPase did not differ between ALS and control patients, suggesting that erythrocyte membranes were normal in ALS. However, the activity of plasma AChE in patients with ALS and PMA was increased significantly over plasma activity in disease controls and normal controls. In addition, in an animal model of human PMA, the Wobbler mouse, plasma AChE activity was increased significantly over littermate controls. The explanation for the increase in plasma acetylcholinesterase was not clear; however, a number of potentially useful clinical points followed from this study. First, there was no relationship between a specific subtype of motor neuron disease and the level of AChE activity. Second, AChE activity appeared to vary directly with the duration of PMA but not with the severity of PMA. This did not correlate with either the duration or severity of ALS. Last, plasma AChE activity was normal in about 30% of patients who had motor neuron disease; therefore, AChE assay had limited use in the diagnosis of ALS or PMA.
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PMID:Acetylcholinesterase and ATPases in motor neuron degenerative diseases. 613 69

A total of 147 muscle spindles was studied histochemically in serial transverse sections of 42 cat tenuissimus muscle specimens. Nuclear bag1, nuclear bag2 and nuclear chain intrafusal muscle fibers were distinguished by the differential staining resulting from the reactions for myosin adenosine 5'-triphosphatase and nicotinamide adenine dinucleotide tetrazolium reductase. The majority of intrafusal fibers were of the same histochemical type at both fiber poles. However, seven muscle spindles contained one nuclear bag fiber each that presented as a bag1 in one pole and as a bag2 in the other pole. These "mixed" nuclear bag fibers were found in spindles that also contained at least one bag1 and one bag2 fiber of equivalent histochemical presentation in both fiber poles. The "mixed" bag fibers displayed differences of apparent fiber diameter and relative polar length between the two fiber poles. The motor innervation pattern, as revealed by staining for cholinesterase, was also dissimilar between the two poles of "mixed" bag fibers. The study indicates that the spindle equatorial region may in some instances serve as a boundary between two morphologically and histochemically different poles of the same intrafusal fiber.
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PMID:The occurrence of "mixed" nuclear bag intrafusal fibers in the cat muscle spindle. 616 92

Cat muscle spindles were studied histochemically in serial transverse sections of the tenuissimus muscle stained for myofibrillar ATPase, cholinesterase or NADH-tetrazolium reductase. The terminal sites of the primary and secondary axons on intrafusal muscle fibers could be demonstrated due to their high NADH-TR activity. This sensory NADH-TR reactivity at the equator and in the juxtaequatorial regions disappeared following spindle chronic de-afferentation, but not after de-efferentation. Spindle poles that carried both primary and secondary sensory endings had a longer periaxial fluid space than poles with primary endings only, and their motor innervation, as determined by staining for ChE, was positioned at the greater distance from the equator. Some of the secondary endings occurred in intrafusal regions that displayed surface fiber ChE activity. The histochemical reaction for NADH-TR represents a simple, rapid and reliable method for studies of the distribution of sensory nerve terminals in the spindle.
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PMID:Appearance of sensory nerve terminals in cat muscle spindles stained for NADH-tetrazolium reductase. 617 8

The foliate papillae of the rabbit, rat and mouse were studied by scanning electron microscopy and histochemistry. The papillae consisted of folds and grooves located on the posterolateral margin of the tongue in front of the circumvallate papillae. The numbers of folds and taste buds varied among the three animals species. Scanning electron microscopy showed that in longitudinal sections the taste buds were oval in shape and their pores were surrounded by microvilli. The reaction product of alkaline phosphatase could only be demonstrated in the superficial epithelium of the rabbit as well as in the mouse foliate papillae, but it also diffused into the taste buds in the rat. The intensity and distribution of the reactions of adenosine triphosphatase, acetylcholinesterase and butyrylcholinesterase were identical to those reported by other investigators in spite of differences in animal species and histochemical techniques employed.
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PMID:Scanning electron microscopic and histochemical studies of foliate papillae in the rabbit, rat and mouse. 621 38

It is shown that myosin of human skeletal muscles is more difficult for purification from the actin and nucleic acids admixtures. It is also characterized by a less yield and a pronounced lability to denaturant effects as compared to rabbit myosin. The ATPase activity of human myosin is 1.5-2 times as low and the cholinesterase one--tens of times as high as those of rabbit myosin. A relative content of LC3 (LC--light chains) is approximately twice as low and that of LC1--as high as in rabbit myosin. It is supposed that the found differences in the properties may be explained to a considerable extent by a different ratio of certain light chains contained in the investigated proteins.
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PMID:[Subunit composition and enzymatic properties of myosins from human and rabbit skeletal muscles]. 621 80

A method of "thin slices" was developed for estimation of enzymatic activities in cells, in which relationship between structure elements was maintained and the cells were readily permeable for substrates. Activities of Na, K-ATPase and succinate dehydrogenase were markedly higher in thin slices than in homogenates; activities of choline esterase and lactate dehydrogenase were of the same value in both tissue preparations. As compared with controls, adrenalectomy caused a decrease in Na, K-ATPase activity in the tissue slices, activities of succinate- and lactate dehydrogenases were unaltered and the choline esterase activity was increased. Comparison of the enzymatic activities in homogenates and thin slices indicates that some contradictions in data on the effect of the adrenal cortex hormones on the activity of the enzymes involved in the ion transport porcesses are due mainly to unadequateness of the methods used.
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PMID:[Effect of adrenalectomy on the enzymatic activity in thin kidney slices and homogenates]. 625 88


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