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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Methanogenesis from formaldehyde or formaldehyde + H2, as carried out by Methanosarcina barkeri, was strictly dependent on sodium ions whereas methane formation from methanol + H2 or methanol + formaldehyde was Na+-independent. This indicates that the reduction of formaldehyde to the formal redox level of methanol exhibits a Na+ requirement. During methanogenesis from formaldehyde, a delta pNa in the range of -62 mV to -80 mV was generated by means of a primary, electron-transport-driven sodium pump. This could be concluded from the following results obtained on cell suspensions of M. barkeri. 1. The addition of proton conductors or inhibitors of the Na+/H+ antiporter had no effect on sodium extrusion. 2. During methanogenesis from formaldehyde + H2 a delta psi of -60 mV to -70 mV was generated even in the presence of proton conductors. 3. ATPase inhibitors, applied in the presence of proton conductors, had no effect on primary sodium extrusion or generation of a delta psi. Evidence for a Na+-translocating ATPase could not be obtained.
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PMID:Electron-transport-driven sodium extrusion during methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri. 285 Jan 82

Immunohistochemical techniques have been used to localize clotting factor XIII subunit A in human reactive lymphoid follicles. The follicular dendritic reticulum cells (DRCs) were identified by the monoclonal antibodies R4/23 and OKB-7 as well as by their 5'-nucleotidase positivity. Follicular histiocytic reticulum cells (HRCs) were demonstrated by their acid phosphatase and non-specific esterase reactions. Capillaries were selectively visualized by adenosine triphosphatase. The immunohistochemical demonstration of F-XIIIa was preferably carried out in combination with one or two of the above marker techniques, on the same cryostat section. The subunit A of factor XIII is present in follicular DRCs. Their selective immunohistochemical demonstration with antibody against F-XIIIa requires formaldehyde fixation of cryostat sections. Similar fixation, however, is inappropriate for the demonstration of F-XIIIa reactivity of DRCs in paraffin sections. For this purpose, acetic acid-formalin fixation is useful. Follicular HRCs are consistently negative for F-XIIIa, contrary to the F-XIIIa positivity of sinusoidal and interfollicular HRCs. Developmental and functional implications of F-XIIIa reactivity in DRCs and HRCs are suggested.
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PMID:Selective visualization of human dendritic reticulum cells in reactive lymphoid follicles by the immunohistochemical demonstration of the subunit A of factor XIII (F-XIIIa). 288 67

The association of an ATPase with the yeast peroxisomal membrane was established by both biochemical and cytochemical procedures. Peroxisomes were purified from protoplast homogenates of the methanol-grown yeast Hansenula polymorpha by differential and sucrose gradient centrifugation. Biochemical analysis revealed that ATPase activity was associated with the peroxisomal peak fractions which were identified on the basis of alcohol oxidase and catalase activity. The properties of this ATPase closely resembled those of the mitochondrial ATPase of this yeast. The enzyme was Mg2+-dependent, had a pH optimum of approximately 8.5 and was sensitive to N,N'-dicyclohexylcarbodiimide (DCCD), oligomycin and azide, but not to vanadate. A major difference was the apparent Km for ATP which was 4-6 mM for the peroxisomal ATPase compared to 0.6-0.9 mM for the mitochondrial enzyme. Cytochemical experiments indicated that the peroxisomal ATPase was associated with the membranes surrounding these organelles. After incubations with CeCl3 and ATP specific reaction products were localized on the peroxisomal membrane, both when unfixed isolated peroxisomes or formaldehyde-fixed protoplasts were used. This staining was strictly ATP-dependent; in controls performed in the absence of substrate, in the presence of glycerol 2-phosphate instead of ATP, or in the presence of DCCD, staining was invariably absent. Similar staining patterns were observed in subcellular fractions and protoplasts of Candida utilis and Trichosporon cutaneum X4, grown in the presence of ethanol/ethylamine or ethylamine, respectively.
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PMID:A proton-translocating adenosine triphosphatase is associated with the peroxisomal membrane of yeasts. 288 51

The enamel organ of the growing rat incisor was fixed with a mixture of formaldehyde and glutaraldehyde and processed for ultracytochemical demonstration of Ca- and Mg-activated membrane ATPase by a one-step lead technique at alkaline pH. To inhibit nonspecific alkaline phosphatase, 5 mM levamisole was added to the incubation media. Intense Ca- and Mg-ATPase activity was demonstrated in the cell surfaces of the secretory ameloblasts, except at the proximal and distal junctional complexes and the gap junctions in the lateral and basal cell surfaces. Deep plasma membrane invaginations at the proximal and distal parts of Tomes processes facing interrod- and rod-enamel growth regions exhibited the strongest enzymatic reaction. Mg-ATPase activity was also shown to be present in the plasma membranes of secretory ameloblasts but it was less intense than Ca-ATPase. Except for a slight reaction in the Golgi membranes, all other cell organelles of the secretory ameloblasts and the adjacent enamel matrix were free of enzymatic reaction. However, when the tissues were incubated in media lacking levamisole, a prominent enzymatic reaction was observed in the newly secreted enamel matrix of the rod and interrod growth regions as well as on the plasma membranes of the cells. In maturation ameloblasts of both ruffle-ended and smooth-ended types, a weak reaction for Ca- and Mg-ATPase was restricted to basal cell surfaces facing the papillary cell layer. In tissues incubated in media lacking levamisole, a variable deposition of reaction products was observed in the Golgi membranes, mitochondrial membranes, tubular elements of smooth endoplasmic reticulum in the ruffled border zone, and along the plasma membranes of the ruffled border. Throughout the secretory and maturation stages, a moderate and/or weak enzymatic reaction for both Ca- and Mg-ATPase was seen in the plasma membranes of the cells of the stratum intermedium and the papillary layer when incubated in media with levamisole. Omission of substrate ATP and/or the enzyme activator CaCl2 from the incubation media for Ca-ATPase produced a negative reaction in the tissues examined. When the calmodulin blocker trifluoperazine was administered to the rats intravenously, Ca-ATPase activity was almost completely abolished from the plasma membranes of secretory ameloblasts, but not of other cell types.
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PMID:Ultracytochemical demonstration of ATP-dependent calcium pump in ameloblasts of rat incisor enamel organ. 294 78

Glutaraldehyde treatment of sarcoplasmic reticulum vesicles results in formation of cross-linked Ca2+-ATPase oligomers. Under limiting reaction conditions, where minimal interpolypeptide cross-linking occurs, hydrodynamic properties of the monomer are altered, such that, on sodium dodecyl sulfate-polyacrylamide electrophoresis, the enzyme migrates with an apparent molecular weight of 125,000 (E(125], as compared to the native enzyme (E(110]. The E(125) species was also formed following reaction with other cross-linking bis-aldehydes, with formaldehyde and with a bissuccinimidyl ester. Derivitization resulted in inactivation of ATPase activity and of phosphoprotein formation from Pi. E(125) formation was inhibited by ATP, ADP, AMPPCP, and orthovanadate, and by specific modification of active site Lys-514 with fluorescein-5'-isothiocyanate. Tryptic cleavage patterns of the glutaraldehyde-modified enzyme were consistent with covalent linkage of A1 and B fragments that have been postulated to comprise the phosphorylation and nucleotide-binding domains (MacLennan, D. H., Brandt, C. J., Korczak, B., and Green, N. M. (1985) Nature 316, 696-700). The denaturing detergent, sodium dodecyl sulfate, prevented cross-link formation. Interdomain cross-linking was inhibited by prior modification with either 2,4,6-trinitrobenzene sulfonate, phenylglyoxal, or pyridoxal-5'-phosphate but was unaffected by thiol group modification with iodoacetate or N-ethylmaleimide, suggesting involvement of lysine residues. These findings indicate that intramolecular cross-linking at the active site of the Ca2+-ATPase involves phosphorylation- and ATP-binding domains that are widely separated in the linear sequence.
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PMID:Intramolecular cross-linking of domains at the active site links A1 and B subfragments of the Ca2+-ATPase of sarcoplasmic reticulum. 295 84

The authors elaborated and described the optimum conditions for fixation, incubation and preparation of human blood cell samples in minimum quantities for ultrastructural and ultracytochemical investigations of 5'-nucleotidase and ATPase activities. The best preservation of the blood cell ultrastructure was obtained after fixation with buffered 1% glutaraldehyde solution followed by postfixation in buffered 1% OsO4 solution. The best ultracytochemical demonstration of 5'-nucleotidase and ATPase activities was achieved after fixation in buffered 2% formaldehyde prior to cytochemical incubation. DMSO added to either fixation or incubation media was shown to damage the plasmalemma and glycocalyx structure in cell suspensions. ATPase in 5'-nucleotidase activities were revealed in plasmalemma, cytoplasmic reticulum, Golgi complex, mitochondria and in the nuclei, in particular, in the perinuclear space, nucleolus and chromatin. With respect to the localization and activity of nucleosidephosphatases, lymphocytes proved to be most heterogenic, with the enzyme activity level directly depending on the rate of ultrastructural differentiation in lymphocytes.
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PMID:[Ultracytochemical detection of nucleoside phosphatase activity in human peripheral blood cells]. 300 81

Sprague-Dawley strain rats of 4-5 weeks old were perfusion-fixed with either a mixture containing 0.1 or 0.25% glutaraldehyde and 2% formaldehyde, or a 2% formaldehyde in 0.1 M sodium cacodylate buffer for 10 minutes. Non-decalcified 30-50-micron sections of the enamel organ taken from lower incisors were then processed for ultracytochemical demonstration of ouabain-sensitive, K+-dependent, p-nitrophenyl phosphatase, by use of the one-step lead method, representing the second dephosphorylative step of Na+-K+-ATPase. Throughout the secretory, transition, and maturation stages of amelogenesis, the enzymatic activity was demonstrated along the cytoplasmic side of the plasma membranes of the stratum intermedium and the papillary layer cells, especially along their numerous microvilli. The plasma membranes forming gap junctions and desmosomes were free of reaction or showed slight focal precipitates of reaction products. The stellate reticulum and the outer enamel epithelium exhibited either a weak reaction or were reaction negative. Secretory ameloblasts showed a weak trace-like reaction along the basal and lateral cell surfaces; however, the latter surfaces were sometimes completely free of reaction. Tomes' processes were usually reaction negative. Ameloblasts in the transition and maturation stages were devoid of enzymatic activity, except for a slight reaction along the plasma membranes of the basal cell surfaces of transition ameloblasts facing the papillary layer. The enzymatic activity described above was completely dependent on the presence of potassium and substrate in the incubation media and was almost completely inhibited by an addition of 10 mM ouabain to the incubation media.
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PMID:Ultracytochemistry of ouabain-sensitive K+-dependent p-nitrophenyl phosphatase in rat incisor enamel organ. 302 Oct 21

The effects of the calmodulin blocker, trifluoperazine (TEP), on membrane-bound Ca++-ATPase, Na+-K+-ATPase (EC 3.6.1.3.) and the ultrastructure of the enamel organ were investigated in the lower incisors of normal and TFP-injected rats. The rats, of about 100 g body weight, were given either 0.2 ml physiological saline or 100 micrograms TFP dissolved in 0.2 ml physiological saline through a jugular vein and fixed by transcardiac perfusion with a formaldehyde-glutaraldehyde mixture at 1 and 2 h after TFP administration. Non-decalcified sections of the enamel organ less than 50 micron in thickness, prepared from dissected lower incisors, were processed for the ultracytochemical demonstration of Ca++-ATPase and Na+-K+-ATPase by the one-step lead method at alkaline pH. In control saline-injected animals the most intense enzymatic reaction of Ca++-ATPase was demonstrated along the plasma membranes of the entire cell surfaces of secretory ameloblasts. Moderate enzymatic reaction was also observed in the plasma membranes of the cells of stratum intermedium and papillary layer. Reaction precipitates of Na+-K+-ATPase activity were localized clearly along the plasma membranes of only the cells of stratum intermedium and papillary layer. The most drastic effect of TFP was a marked disappearance of enzymatic reaction of Ca++-ATPase from the plasma membranes of secretory ameloblasts, except for a weak persistent reaction in the basolateral cell surfaces of the infranuclear region facing the stratum intermedium. The cells of stratum intermedium and papillary layer, however, continued to react for Ca++-ATPase even after TFP treatment.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Calmodulin blocker inhibits Ca++-ATPase activity in secretory ameloblast of rat incisor. 303 46

The distribution of several hydrolytic enzymes was investigated in rabbit submandibular glands at both the light and electron microscopical levels. Glands were fixed by either immersion or perfusion fixation with a variety of fixatives containing 1-2% glutaraldehyde and 2-4% formaldehyde in 0.1 M cacodylate buffer at pH 7.2. Light microscopically, the acinar cells showed some staining for ATPase, acid phosphatase and nonspecific esterases but showed weak staining for thiamine pyrophosphatase. Acid phosphatase staining occurred most strongly in granular tubule cells. Staining for esteroproteases was confined to the periluminal rims of intercalary and striated ducts. Alkaline phosphatase was very sensitive to glutaraldehyde and was confined to myoepithelial cells. Electron microscopical observations revealed the presence of acid phosphatase reaction product in lysosomes, immature granules and in GERL-like structures, the last being much more conspicuous in the granular tubule cells. ATPase reaction product was localized to the basal and luminal plasma membranes and lumina of both acinar and granular tubule cells. The Golgi complex of these two types of cells exhibited only moderate amounts of reaction product for thiamine pyrophosphatase. Alkaline phosphatase activity, on the other hand, was exclusively localized to myoepithelial cells in their plasma membranes and sometimes in the nuclear envelope.
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PMID:Histochemistry of hydrolytic enzymes in resting submandibular glands of rabbits. 316 50

The washed cells of Hansenula polymorpha and Pichia pinus grown on the medium with methanol rapidly acidify the medium during incubation with the mentioned alcohol or formaldehyde. It is found that proton extrusion is coupled with formate anion efflux. Acidification is proved to be energy-dependent process since it is inhibited by respiration poisons, uncouplers of oxidative phosphorylation, and by ATPase inhibitors.
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PMID:[The nature of methanol-induced acidification of the medium by products of metabolism of methylotrophic yeasts]. 328 21


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