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

When temperature differences are taken into account, turtle brains use glucose at one-sixth the rate reported in rat brains. Na+-K+-ATPase activities are 2- to 2.5-fold higher in rat than in turtle brains. Maximal activities of hexokinase and lactate dehydrogenase are similar, whereas citrate synthase activities are two- to threefold higher in rat than turtle brains at the respective biological temperatures. Voltage-dependent Ca2+ channel densities, when compared between the two species, showed no consistent pattern. These data, along with the threefold differences in density of voltage-dependent Na+ channels reported by Lutz et al., are consistent with the idea that lower rates of channel and pump-mediated Na+ and K+ fluxes result in lower rates of aerobic energy metabolism in turtle brains compared with rat brains.
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PMID:Turtles and rats: a biochemical comparison of anoxia-tolerant and anoxia-sensitive brains. 255 54

Langerhans' cells (LCs) appear to be altered in diseases that express a depressed cellular immune response. We measured the density of LCs in the skin of patients with the disseminated form of paracoccidioidomycosis. The study was performed using adenosine triphosphatase staining of epidermal sheets. Sixteen patients with paracoccidioidomycosis were evaluated. They had a highly significant reduction in LCs (LCs, 323 +/- 135/mm2) when compared with the number (LCs, 689 +/- 204/mm2) found in the control subjects. Morphological alterations of these cells were noted in patients with low numbers of LCs. These findings may reflect the depressed cellular immunity secondary to the infection with Paracoccidioides brasiliensis.
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PMID:Langerhans' cells in paracoccidioidomycosis. 382 79

Different classes of tryptophan residues in sarcoplasmic reticulum calcium-ATPase were investigated with respect to their exposure to quenchers and sensitivity to high-affinity calcium binding to the ATPase. The charged quenchers, iodide and cesium, produced only slight quenching of ATPase fluorescence, whereas noncharged acrylamide and notably oxygen produced significant quenching. This finding gives support to the proposed location of most of the tryptophan residues of the ATPase in transmembrane domains of this protein (MacLennan et al., 1985, Nature 316r, 696-700). Among the different quenchers tested, oxygen quenching alone was sensitive to calcium binding to the ATPase, indicating that oxygen quenched tryptophan residues located in regions of the ATPase molecule which undergo conformational changes upon calcium binding. Time-resolved oxygen quenching data were analyzed with a recently described model that takes into account the existence of two different classes of emitters in the ATPase (Ferreira and Verjovski-Almeida, 1991, J. Lumin. 48, 430-434): a short-lived blue-shifted exponential component plus a long-lived red-shifted continuous lifetime distribution. Oxygen quenching of the single-exponential lifetime component was found to be insensitive to calcium, whereas quenching of the distributed lifetime component was significantly (ca 25%) enhanced by calcium binding. The different sensitivities of the two tryptophan classes to calcium binding to the ATPase are interpreted in terms of the proposed location of tryptophan residues in relation to the calcium transport sites in the ATPase molecule.
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PMID:Fluorescence lifetime and quenching studies of sarcoplasmic reticulum Ca(2+)-adenosine-5'-triphosphatase. 841 9