K Atpase Subunits
Mostrando 1-12 de 141 artigos, teses e dissertações.
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1. Mechanism of association of Na,K-ATPase subunits studied by chemical and physical agents: comparison between solubilized and liposome reconstituted enzyme. / Mecanismos de dissociação das subunidades alfa e Beta da Na,K-ATPase por agentes químicos e físicos: comparação entre a enzima solubilizada e reconstituída em lipossomos
A Na,K-ATPase é uma proteína encontrada na membrana plasmática de praticamente todas as células animais, que utiliza a energia derivada da hidrólise do ATP para transportar 3 íons Na+ e 2 íons K+. É composta por duas subunidades denominadas e . Um aspecto que ainda gera controvérsias se refere à sua forma de associação nativa e funcional como um
Publicado em: 2007
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2. The alpha subunit of the Na,K-ATPase specifically and stably associates into oligomers.
The Na,K-ATPase is a heterodimer consisting of an alpha and a beta subunit. Both Na,K-ATPase subunits are encoded by multigene families. Several isoforms for the alpha (alpha 1, alpha 2, and alpha 3) and beta (beta 1, beta 2, and beta 3) subunits have been identified. All these isoforms are capable of forming functionally active enzyme. Although there is gen
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3. Differential expression and enzymatic properties of the Na+,K(+)-ATPase alpha 3 isoenzyme in rat pineal glands.
We have used immunoblotting and biochemical techniques to analyze expression of Na+,K(+)-ATPase alpha and beta subunits in rat pineal glands. Western blot analysis of pineal microsomal membrane fractions with antisera specific for each of the three rat alpha and two rat beta subunits revealed similar levels of expression of alpha 1 and alpha 3 subunits in pi
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4. Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes.
Active transport across the vacuolar components of the eukaryotic endomembrane system is energized by a specific vacuolar H+-ATPase. The amino acid sequences of the 70- and 60-kDa subunits of the vacuolar H+-ATPase are approximately equal to 25% identical to the beta and alpha subunits, respectively, of the eubacterial-type F0F1-ATPases. We now report that t
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5. Sensitivity to vanadate and isoforms of subunits A and B distinguish the osteoclast proton pump from other vacuolar H+ ATPases.
Analysis of proton (H+) transport by inside-out vesicles derived from highly purified chicken osteoclast (OC) membranes has revealed the presence of a newly discovered type of vacuolar H+ ATPase (V-ATPase). Unlike vesicles derived from any other cell type or organelle, H+ transport in OC-derived vesicles is sensitive to V-ATPase inhibitors (N-ethylmaleimide
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6. Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila.
A new isolate of the aceticlastic methanogen Methanothrix thermophila utilizes only acetate as the sole carbon and energy source for methanogenesis (Y. Kamagata and E. Mikami, Int. J. Syst. Bacteriol. 41:191-196, 1991). ATPase activity in its membrane was found, and ATP hydrolysis activity in the pH range of 5.5 to 8.0 in the presence of Mg2+ was observed. I
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7. Functional expression of the alpha 2 and alpha 3 isoforms of the Na,K-ATPase in baculovirus-infected insect cells.
Multiple isoforms of both the alpha and beta subunits of Na,K-ATPase have been identified. Elucidating their roles has been complicated by the fact that most tissues express multiple isoforms and purification techniques specific for each isoform have not been achieved. The baculovirus expression system, which uses the baculovirus Autographica californica to
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8. Mutational analysis of yeast vacuolar H(+)-ATPase.
Yeast mutants in which genes encoding subunits of the vacuolar H(+)-ATPase were interrupted were assayed for their vacuolar ATPase and proton-uptake activities. The vacuoles from the mutants lacking subunits A (72 kDa), B (57 kDa), or c (proteolipid, 16 kDa) were completely inactive in these reactions. Immunological studies revealed that in the absence of ea
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9. Purification and Properties of the F1Fo ATPase of Ilyobacter tartaricus, a Sodium Ion Pump
The ATPase of Ilyobacter tartaricus was solubilized from the bacterial membranes and purified. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed the usual subunit pattern of a bacterial F1Fo ATPase. The polypeptides with apparent molecular masses of 56, 52, 35, 16.5, and 6.5 kDa were identified as the α, β, γ, ɛ, a
American Society for Microbiology.
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10. Isolation of subunits from Methanosarcina barkeri ATPase: nucleotide-binding site in the alpha subunit.
The alpha (62,000-dalton) and beta (49,000-dalton) subunits of Methanosarcina barkeri ATPase were purified to homogeneity. The subunits and ATPase complex were trypsinized in the presence of various nucleotides. ATP and ADP changed the trypsin sensitivity of the alpha subunit in the complex and isolated forms, suggesting the presence of a nucleotide-binding
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11. Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex.
The yeast vacuolar proton-translocating ATPase (V-ATPase) is a multisubunit complex comprised of peripheral membrane subunits involved in ATP hydrolysis and integral membrane subunits involved in proton pumping. The yeast vma21 mutant was isolated from a screen to identify mutants defective in V-ATPase function. vma21 mutants fail to assemble the V-ATPase co
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12. Initial Steps in the Assembly of the Vacuole-Type H+-ATPase1
The plant vacuole is acidified by a complex multimeric enzyme, the vacuole-type H+-ATPase (V-ATPase). The initial association of ATPase subunits on membranes was studied using an in vitro assembly assay. The V-ATPase assembled onto microsomes when V-ATPase subunits were supplied. However, when the A or B subunit or the proteolipid were supplied individu
American Society of Plant Physiologists.