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)

Coronal odontoblast-predentin tissue was taken from intact teeth and from teeth with carious lesions of varying depths, and the samples (20, 200 x g, saline-soluble fractions) were studied for their ability to hydrolyze adenosine triphosphate (ATP) and phosphoserine. A significantly higher rate of ATP hydrolysis at pH 9.8 was detected in enamel caries and a significantly lower rate in advanced caries than in intact teeth. The rates of the hydrolysis of phosphoserine at pH 9.8 did not differ between the various tooth groups, and the only clear trend indicating elevated enzyme activity was seen in the group of initial dentin caries. The ATP and phosphoserine hydrolysis at pH 9.8 were considered to have been due to the nonspecific alkaline phosphatase (EC 3.1.3.1) activity. In the presence of both levamisole and ouabain, maximal enzyme-dependent ATP hydrolysis was observed at pH 7.9. The remaining ATP-cleaving activity was thought to have been due to the Ca2+Mg2+-dependent ATPase (EC 3.6.1.3). The Ca2+Mg2+-dependent ATPase activities at pH 7.9 remained at constant levels in both the intact and carious groups. The parameters studied in vitro were thought to reflect changes in the mineralization rate of reparative dentin as a response to caries in vivo.
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PMID:The hydrolysis rates of ATP and phosphoserine in the odontoblast-predentin region of intact and carious human teeth. 4 67

The histochemical distribution of 14 enzymes in the human amnion at term are described. Adenosine triphosphatase, 5'-nucleotidase, acid phosphatase and nonspecific esterase show continuous gradations of enzyme activity. Cells with intense activity are prominent in acid phosphatase and nonspecific esterase preparations. A distinct subpopulation of amniotic cells can be defined by their alkaline phosphatase activity. The possible correlations with morphological studies are discussed.
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PMID:Enzyme histochemical patterns in the normal human amnion: amniotic histochemical patterns. 4 99

Plasma membranes from normal, full-term human placental trophoblast have been isolated by a new procedure. The method depends upon isopycnic zonal centrifugation using linear sucrose/Ficoll density gradients. Enrichment of plasma membrane marker enzymes with respect to trophoblast homogenate is found in two distinct peaks (designated B and D) of the fractionated effluent recovered from the rotor. Fraction B is enriched with membrane-bound alkaline phosphatase and 5'-nucleotidase, but not with (Na+, K+)-ATPase of F(-)-stimulated adenylate cyclase. It is suggested that this material is derived from the maternal-facing microvillous plasma membrane. Fraction D, enriched with (Na+, K+)-ATPase, F(-)-stimulated adenylate cyclase and, to a smaller extent, with 5'-nucleotidase and alkaline phosphatase is, by exclusion, proposed to be derived from the fetal-facing basal plasma membrane. Both plasma membrane fractions are shown to be free of appreciable contamination, using specific markers for endoplasmic reticulum, mitochondria, nuclei and lysosomes. The separation of the two membrane fractions is shown to depend both upon these membranes forming closed vesicles during homogenization and upon the buoyant densities of such vesicles differing in such a way that microvillous plasma membranes band at a lower density than basal plasma membranes. No separation of the membranes is achieved in gradients in which the vesicles are collapsed.
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PMID:Separation of the microvillous (maternal) from the basal (fetal) plasma membrane of human term placenta: methods and physiological significance of marker enzyme distribution. 9 48

Sorbitol density gradient centrifugation applied to intestinal mucosa homogenates resulted in a complete separation of soluble calcium-binding protein from the bound fraction of calcium-binding protein, providing further documentation of the bound pool of calcium-binding protein. The peak of the bound calcium-binding protein was not associated with the major peaks of any of the markers used, but was associated with minor peaks of alkaline phosphatase, RNA, and glucose-6-phosphatase. Lack of association of bound calcium-binding protein with (Na+ + K+)-ATPase indicated that the bound calcium-binding protein is not on the basolateral membrane. Differential centrifugation fractionation indicated that the bound calcium-binding protein is not associated with nuclei or mitochondria. The bound calcium-binding protein also could not be detected in partially purified brush borders. Exclusion of the brush border and basolateral membranes as the location of the bound calcium-binding protein suggests an intracellular locale.
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PMID:Studies on the subcellular localization of the membrane-bound fraction of intestinal calcium-binding protein. 11 17

The biochemical effects of the nonsteroidal compound Centchroman were observed in healthy, adult, female rhesus monkeys. The compound was administered at the antifertility dose (.625 mg/kg) for 22 days in a cycle. No marked weight changes were seen in the Fallopian tube, ovary, adrenal or pituitary as a result of treatment. Uterine weight increased significantly, however (p less than .01). In the Fallopian tube, levels of glycogen and protein increased significantly (p less than .01), lactic acid decreased significantly (p less than .01), and nonprotein nitrogen was unchanged as a result of treatment. Similar changes were observed in the uterus, and in addition, total total phospholipid concentration rose significantly (p less than .01) in the uterus. The activities of beta-glucuronidase, acid and alkaline phosphatases and glucose-6-phosphate dehydrogenase (G-6-PD) in the Fallopian tube were unchanged due to treatment. Adenosine triphosphatase (ATPase) and malic dehydrogenase activities were significantly stimulated (p less than .01) and lactic dehydrogenase activity was significantly depressed (p less than .01). In the uterus, beta-glucuronidase and acid and alkaline phosphatase activity were unaltered, however, the activities of ATPase and the dehydrogenases of glucose-6-phosphate, lactate and malate were markedly increased (p less than .01). It is suggested that the antifertility effect of Centchroman may be due principally to the ability of the compound to elicit estrogen-like responses in the Fallopian tube and uterus.
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PMID:Effect of 3,4-trans-2,2-dimethyl-3-phenyl-4-P-(beta-pyrrolidinoethoxy) phenyl -7-methoxy chroman (centchroman) on the biochemistry of the fallopian tube and uterus of rhesus monkeys (Macaca mulatta). 12 88

The effects of the nonsteroidal title compound (DBF) on the biochemical composition of the Fallopian tube and uterus were studied in the rhesus monkey. Monkeys received 2 mg/kg daily by mouth, which is the antifertility dose. The weight of the pituitary was significantly decreased (p less than .05) due to treatment, but the weights of the Fallopian tube, uterus, ovary and adrenal were unaltered. In both the Fallopian tube and uterus, DBF induced a significant increase (p less than .01) in the concentration of glycogen, protein and nonprotein nitrogen, and a significant decrease (p less than .01) in the concentration of lactic acid. The total phospholipid level in the uterus showed an increase (p less than .01) in the activities of adenasine triphosphatase (ATPase), malic dehydrogenase, acid and alkaline phosphatases, and glucose-6-phosphate dehydrogenase (G-6-PD) was seen. Lactic dehydrogenase activity fell (p less than .01) and the activity of beta-glucuronidase was unchanged. In the uterus, ATPase, malic dehydrogenase, alkaline phosphatase and lactic dehydrogenase activities increased significantly (p less than .01), beta-glucuronidase and acid phosphatase activities fell (p less than .01) and G-6-PD activity was unaltered. The antifertility effect of DBF may be due to its ability to elicit many biochemical effects similar to those induced by a typical estrogen.
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PMID:Effect of 2-phenyl-3-p-(beta-pyrrolidinoethoxy) phenyl-beta-methoxy benzofuran hydrochloride (DBF) on the biochemistry of the fallopian tube and uterus of rhesus monkey (Macaca mulatta). 12 89

Bone ECF is separated from the general ECF by a functional membrane which has been shown to limit the mineralization of embryonic tibiae and to selectively pump Ca out of the bone ECF. Energy to run this pump may be derived from ATP hydrolyzed by Ca-2+-stimulated ATPase, an enzyme activity which bone alkaline phosphatase may possess. The data suggest that PTH rapidly and selectively increases Ca pumping possibly by increasing ATPase activity in the bone cell cytosol through increased Ca influx and by increasing the intracellular ATPase level through inhibited secretion or excretion of the enzyme.
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PMID:Cellular control of calcium movements in bone. Interrelationships of the bone membrane, parathyroid hormone and alkaline phosphatase. 12 41

A histochemical study of the effect of ischaemia on rat kidneys showed that changes were demonstrable in adenosine triphosphatase, alkaline phosphatase and succinic dehydrogenase within 2 h. Further changes occurred with increasing time. The activity of acid phosphatase was little affected up to 24 h although at this time there was marked tubular disruption. Paraffin embedded H and E sections also showed marked changes within 2 h. Enzyme histochemical and histological changes in kidneys taken at varying periods after the death of the animal showed very similar changes to those in ischaemic kidneys. Differences were mainly in the rate and extent of the changes.
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PMID:A comparative enzyme histochemical and histological study of the effect of ischaemia and post mortem change on rat kidneys. 12 48

1. Six rat liver plasma-membrane subfractions of different density and morphological, enzymic and chemical properties were prepared from homogenates by a combination of differential, rate-zonal and density-gradient centrifugation. They consisted of three vesicular 'light' subfractions of density 1.12-1.13 and three 'heavy' subfractions of density 1.16-1.18 containing membrane strips and intercellular junctions. 2. All six subfractions contained a basal adenylate cyclase activity. One of the 'light' subfractions that showed the highest glucagon-stimulated adenylate cyclase activity was identified as deriving form the blood-sinusoidal face of the hepatocyte. This subfraction, unlike the others, was contaminated by Golgi components, as indicated by its morphological properties and the presence of galactosyl- and sialyl-transferase activities. 3. All the six subfractions showed high activities of the following plasma-membrane marker enzymes: 5'-nucleotidase, alkaline phosphodiesterase (nucleotide pyrophosphatase), alkaline phosphatase, leucine naphthylamidase and Mg2+-activated adenosine triphosphatase. A 'light' subfraction that showed the highest specific activities of all the above marker enzymes, but lacked a glucagon-stimulated adenylate cyclase activity, was identified as deriving from the bile-canalicular face of the hepatocyte. 4. The 'heavy' subfractions, which showed generally the lowest activities of the above plasma-membrane enzyme markers, and were characterized by the presence of desmosomes and gap junctions, were taken to originate from the contiguous faces of the hepatocyte. 5. The protein composition of the six subfractions was generally similar, as shown by polyacrylamide-gel electrophoresis. Differences in the amounts of various protein and glycoprotein bands among the subfractions correlated with their morphology, enzymic composition and sialic acid content. 6. Hormonal and histochemical evidence supporting the identification of a bile-canalicular subfraction, a blood-sinusoidal subfraction and contiguous-face subfractions is discussed.
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PMID:Functional polarity of the rat hepatocyte surface membrane. Isolation and characterization of plasma-membrane subfractions from the blood-sinusoidal, bile-Canalicular and contiguous surfaces of the hepatocyte. 12 84

Rats were given a single dose of aflatoxin B1 lethal to 50% of the animals (7.20 mg/kg). Their livers were examined histochemically in correlation with sequential histological lesions. Early periportal liver cell necrosis and marked biliary cell proliferation were observed. Periportal cytoplasmic glycogen and RNA depletion occurred during this early period and subsequently extended to the whole lobule. The enzymes investigated decreased or disappeared in the periportal area; but alkaline phosphatase increased strikingly in the centrolobular area, whereas canalicular adenosinetriphosphatase completely disappeared throughout the liver lobule. The histochemical changes reverted to normal after cessation of the necrosis. Histochemical techniques were more sensitive in detecting the vulnerability of the periportal parenchyma to aflatoxin. After the necrosis, regenerative foci appeared. They showed a variable content in glycogen and RNA and were characteristically enzyme deficient. This reflects the immaturity of regenerating hepatocytes. These early foci subsequently disappeared and are thus considered irrelevant to hepatomagenesis.
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PMID:Sequential histological and histochemical study of the rat liver after single-dose aflatoxin B1 intoxication. 12 26


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