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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present studies concern the roles of synthesis and degradation of the large subunit of (Na+ + k+)-adenosine triphosphatase (NaK-ATPase) in the response to triiodothyronin (T3). Single doses of either the diluent of T3 (50 mug/100 g body weight) were given to two pairs of surgically thyroidectomized rats. Twenty hours after injection, the rats received 3H- or 35S-labeled methionine administered as a constant injusion into the tail vein for 1 h. The kidneys were removed either 8 h or 20 h after infusion and the eight kidneys were divided into pairs, as follows. I, 3H (diluent)/35S (T3); II, 35S (diluent)/3H (T3); III, 3H (diluent)/35S (diluent); IV, 3H (T3)/35S (T3). Partially purified NaK-ATPase was prepared from the pooled homogenates and prepared from the pooled homogenates and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAG-electrophoresis). The large subunit of NaK-ATPase was identified by (Na+ + mg2+)-dependent and K+-sensitive incorpotation of 32P from [gamma-32P]ATP. This component had an estimated molecular weight of 92,000 and migrated as a single peptide in gels of varying total carylamide concentration, with respect to: (1) Coomassie blue staining, (b) (Na+ + Mg2+)-dependent, K+-sensitive incorporation of 32P from [gamma-32-P]ATP, and (c) T3-dependent enhanced incorporation of labeled methionine. T3 augmented incorporation of labeled methionine into the large subunit by 44% 8 h after infusion of the amino acid and by 61% 20 h after infusion. Incorporation of methionine into two adjacent polypeptides in the SDS gels was unaffected by thyroid status. The effect otical NaK-ATPase was assessed by a double label technique. Pairs of thyroidectomized rats were injected with either the diluent or 50 mug of T3/100 g body weight at 48-h after the first injection (diluent or T3, i.e. Day "zero"). Kidney cortices were processed on either Day 4 or Day 6; the partially purified NaK-ATPase fraction was prepared, labeled with [gamma-32P]ATP, and analyzed by SDS-PAG-electrophoresis. The degredation rate constants of the large subunit were similar; 0.145 and 0.124 day-1 for the hypothyroid and T3-treated groups, respectively. Thus, the T2-dependent increase in incorporation of labeled methionine into the large subunit appears to result from enhanced synthesis and this increase is sufficient to account for the entire increase in both the number of the activity of the NaK-ATPase units.
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PMID:Effect of triiodothyronine on the synthesis and degradation of renal cortical (Na+ + k+)-adenosine triphosphatase. 13 43

Membrane-bound and free polyribosomes were isolated from skeletal muscle of neonatal rats and messages were translated in a rabbit reticulocyte lysate treated with Ca2+ -dependent nuclease to reduce endogenous messenger translation. Newly synthesized calsequestrin and adenosine triphosphatase (ATPase) sere isolated by antibody precipitation, followed by separation of the precipitates in SDS-polyacrylamide gels. Radioactivity in calsequestrin and the ATPase were counted in gel slices. Calsewuestrin and the ATPase were both found to be synthesized on membrane-bound polyribosomes. Since calsequestrin is a glycoprotein, localized in Golgi regions in early stages of muscle cell differentiation, it is probable that its synthesis follows the pathway for synthesis of secreted proteins except that its destination is the luminal space of a cellular organelle. The disposition of the ATPase during synthesis is, as yet, unknown.
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PMID:Assembly of the sarcoplasmic reticulum. Synthesis of calsequestrin and the Ca2+ + Mg2+ -adenosine triphosphatase on membrane-bound polyribosomes. 14 86

Surface antigens of adult filarial parasite S. digitata was isolated by employing techniques from manual dissection to treatment with detergents. Among the surface antigen preparations (SAPs), the activities of marker enzymes such as alkaline phosphatase, adenosine triphosphatase and 5' nucleotidase were higher with that isolated by triton X-100 technique (SAP2). On SDS-PAGE, the SAP2 has three major proteins with molecular weights 17, 29 and 36 KD which were consistent with the PBS soluble cuticular proteins (SAP1). Besides these, few other minor protein bands were also observed with the other SAPs. All SAPs were antigenic and showed positive reaction against antiserum to SAP2, and the results confirmed the SAP2 as a better preparation. The release of 29 KD surface protein during in vitro culture of adult parasite and its cross-reactivity with antiserum to surface antigens revealed the possible natural shedding of surface molecules into the host system.
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PMID:Isolation and analysis of surface antigens of filarial nematode Setaria digitata. 176 14

Skeletal muscle fibers from muscular dystrophic mice (C57BL/10-mdx) 1-4 months of age show elevated free Ca2+ concentrations both at resting and stimulated states, although contractility of adult (2-12 months old) mouse is similar to that of normal mouse. To evaluate the sensitivity of the contractile system of adult mdx mouse muscle to elevated free Ca2+ concentration, Mg2(+)-adenosine triphosphatase (ATPase) activity was examined using myosin, myosin B, and reconstituted actomyosin. Myosin Mg2(+)-ATPase activity of the mdx mouse was significantly higher than that of the normal mouse. Myosin B ATPase activity of the mdx mouse was also higher than that of normal mouse in free Ca2+ concentrations between 10(-9) and 10(-5) M, though there was no difference in the Ca2+ concentration required for half maximal activation of ATPase activity, 2 x 10(-7) M. Polymerized actin (FA) isolated from normal and mdx mice activated rabbit myosin Mg2(+)-ATPase identically, while activation of Mg2(+)-ATPase in mdx myosin by rabbit FA was significantly lower than that in normal mouse myosin. Rapid Pi liberation by Mg2(+)-ATPase in mdx mouse myosin was about half that of normal mouse myosin, being consistent with low activation of Mg2(+)-ATPase activity by rabbit FA. Polyacrylamide gel electrophoresis in the presence of pyrophosphate showed that myosin molecules of mdx and normal mice were both composed of three isozymes, although the fast migrating myosin isozyme (M1) was decreased while the slow migrating band (M3) was increased in mdx myosin. Subunit composition of myosin analyzed by polyacrylamide gel electrophoresis in the presence of SDS showed that the content of the smallest light chain (LC3) in mdx myosin was lower than that of normal mouse myosin, which agreed with findings that mdx myosin contained less M1 isozyme than normal myosin. These results indicated that the lowered response of mdx muscle fibers to elevated Ca2+ concentration can be attributed to the isozyme composition of myosin in mdx mouse.
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PMID:Kinetic properties and isozyme composition of myosin in the mdx mutant mouse. 214 75

Isomyosin analyses by biochemical, immunochemical, and histochemical investigations have been carried out in five sheep following unilateral recurrent laryngeal nerve paralysis and direct functional electrostimulation of the denervated cricoarytenoid posterior muscle. Myosin light chains were identified by two-dimensional gel electrophoresis. Myosin heavy chains were analyzed by one-dimensional SDS-polyacrylamide gel electrophoresis. Slow myosin heavy chain was identified by orthogonal peptide mapping and immunochemistry. The stimulation effect at cellular level was determined using adenosine triphosphatase (ATPase) histochemistry. A dramatic increase of the type 1 fiber area (slow, fatigue-resistant fibers) could be seen after many weeks of an increasing regime of low-frequency direct electrical stimulation. Biochemically, the amount of slow myosin was always higher than in normal muscles. Some muscles were transformed almost completely to the slow type. At the time they were studied and with the methods employed, the expression of embryonic isomyosin was not observed. In conclusion, after numerous weeks of maintained functional activity, elicited by direct electrostimulation, the denervated muscle regionally showed areas of hypertrophy or at least lack of atrophy of slow myofibers without major signs of muscle damage.
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PMID:Isomyosin changes after functional electrostimulation of denervated sheep muscle. 297 27

Several approaches were adopted for the disruption and removal of the tegumental surface from protoscoleces of the horse strain of the hydatid organism, Echinococcus granulosus. The effectiveness of each method and the purity of subsequent microthrix-enriched fractions obtained by differential centrifugation were evaluated by electron microscopy, by the amount of protein released and by the degree of enrichment of surface plasma membrane marker enzymes. Incubation in saponin for 10 min produced the purest microtriche preparation, but in low yield; freeze/thawing, incubation in Triton X-100 for 10 min or in saponin for 20 min produced fractions containing significant amounts of relatively pure microtriches, but mild homogenization was a poor method for surface disruption and subsequent isolation of microtriches. Phosphodiesterase, adenosine triphosphatase (total and ouabain-inhibited), leucine aminopeptidase and glutamyltransferase were active in the protoscoleces but none were enriched in any of the microthrix fractions. In contrast, alkaline phosphatase, acid phosphatase, 5' nucleotidase and maltase were enriched significantly in all of the isolated microtriche preparations, which suggests that these enzymes are predominantly surface membrane bound. The protein profiles of the microthrix-enriched fractions, following SDS-PAGE, were basically similar, although there were some qualitative and quantitative differences in the proteins released by each isolation procedure. Three major PAS-staining components were present in all the preparations and these probably originated from the glycocalyx. One of these PAS-positive components, with an approximate molecular weight of 110 kDa, may be a glycoprotein specific to the horse strain of E. granulosus.
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PMID:Isolation, fractionation and partial characterization of the tegumental surface from protoscoleces of the hydatid organism, Echinococcus granulosus. 398 50

In order to get precise information about the movement of plasma membrane proteins in cap formation, cyto- and bio-chemical analyses were made of the plasma membranes from non-capped areas of Ehrlich ascites tumor cells (EATCs) exposed to concanavalin A (Con A). Blebs formed by treatment with cytochalasin B (CB) of the non-capped areas of cells having a cap were isolated and used as the plasma membranes from non-capped areas (ConA-CB-bleb fraction). This bleb fraction was compared with a bleb fraction prepared from cells without ConA-treatment (CB-bleb fraction). Cytochemical analysis of ConA-CB-bleb fraction revealed a decreased in conA binding sites (ConA-BS) compared to the CB-bleb fraction. SDS polyacrylamide slab gel electrophoresis also revealed a decrease in the major components of ConA-BS of the ConA-CB-bleb fraction. The minor components of ConA-BS showed no distinct quantitative difference between the ConA-CB-bleb and CB-bleb fractions. NA+ K+-adenosine triphosphatase (ATPase), 5' nucleotidase (5'ND) and gamma-glutamyl transpeptidase (gamma-GTP) did not show any decrease in activity in the ConA-CB-bleb fraction, but the activity of D+-stimulated phosphatase (K-Pase) was decreased. The findings indicate that there are two types of plasma membrane glycoproteins in EATCs; one includes those participating in cap formation due to ConA, e.g. the major components of ConA-BS and K-Pase, and the other, those not participating in such cap formation, e.g. some minor components of ConA-BS, ATPase, 5'ND and gamma-GTP, which keep their places without moving.
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PMID:Movement of plasma membrane proteins of Ehrlich ascites tumor cells in relation to cap formation induced by concanavalin A: a study on the non-capped areas. 611 90

Electron spin resonance, enzymatic, and SDS-polyacrylamide gel electrophoretic investigations of erythrocyte membranes from patients with Alzheimer's disease were performed. Alterations in the physical state of membrane proteins in Alzheimer's disease erythrocytes were found by spin labeling studies. However, no alterations in membrane lipid fluidity or in the activities of membrane-bound sodium plus potassium-stimulated, magnesium-dependent adenosine triphosphatase or acetylcholinesterase could be demonstrated. Also, no changes in staining profiles of AD erythrocyte membrane proteins subjected to electrophoresis were observed. The altered conformation and/or organization of extraneural membrane proteins in Alzheimer's disease suggests the possibility that this disorder may have more widespread membrane involvement than was originally thought.
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PMID:Spin label and biochemical studies of erythrocyte membranes in Alzheimer's disease. 624 87

The molecular weight and stoichiometry of the subunits of the sodium- and potassium-activated adenosine triphosphatase. (Na,K)-ATPase, have been examined in four highly purified preparations of this enzyme: dog kidney, eel electroplax, dogfish rectal gland, and brine shrimp nauplius. The molecular weights of the subunits were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) at 10 different total acrylamide concentrations (%T) and by a gradient SDS-PAGE system, standardized with 16 molecular weight marker proteins of known primary structure. The molecular weight of the large (Na,K)-ATPase subunit (alpha subunit) was found to be reliably estimated by SDS-PAGE, whereas the small subunit (beta subunit) was not. The molecular weight of the alpha subunit was 97,000, 97,700, 104,200, and 97,800 for the dog, eel, dogfish, and brine shrimp (Na,K)-ATPase, respectively. The molecular weight of the beta subunit is overestimated by SDS-PAGE. Mass ratio analysis of the alpha and beta subunits separated by SDS-PAGE was determined by three techniques: total amino acid quantitation, gel scanning and dye elution of Coomassie blue-stained gels, and UV gel scanning. The former method, which provides the most reliable estimate of the mass ratio, gives an alpha/beta mass ratio of 2.41, 2.33, 2.91, and 2.44 for the dog, eel, dogfish, and brine shrimp preparations, respectively. Results of the mass ratio studies, the molecular weight analysis, and prior cross-linking studies clearly demonstrate that the quaternary structure of the (Na,K)-ATPase is an alpha 2 beta 2 tetramer in all four species. Based on all of the above data, a more reliable molecular weight estimate of the beta subunit is calculated as 40,200, 43,000, 35,800, and 40,100 for the dog, eel, dogfish, and brine shrimp preparations, respectively. These results now confirm that the molecular weight of the protein portion of the alpha subunit is near 100,000 and that of the beta subunit is near 40,000 and that the (Na,K)-ATPase holoenzyme is an alpha 2 beta 2 tetramer of molecular weight 274,000 to 280,000, regardless of species.
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PMID:Molecular weight and stoichiometry of the sodium- and potassium-activated adenosine triphosphatase subunits. 626 Jul 77

The isolation of basolateral membranes from rat proximal colonic epithelial cells is described. Cells were harvested using a technique combining chelation of divalent cations with mechanical dissociation. After homogenization, differential centrifugation yielded a 'crude' membrane fraction which was further purified using sucrose density centrifugation. The final membrane fraction was enriched 10-14-fold over homogenate in ouabain-sensitive sodium-potassium dependent adenosine triphosphatase and ouabain-sensitive potassium-dependent phosphatase specific activities. SDS-polyacrylamide gel electrophoresis of this membrane revealed at least 18 protein bands with molecular weights of 14600-200000. Phosphatidylcholine, phosphatidylethanolamine, sphingomyelin, free cholesterol and fatty acids were the major lipid components of this membrane. The predominant fatty acids were palmitic (16:0), oleic (18:1), stearic (18:0) and linoleic (18:2) acid. Membranes and their liposomes were studied, using the lipid soluble fluorophore 1,6-diphenyl-1,3,5-hexatriene (DPH), by steady-state fluorescence polarization. The fluorescence anisotropy was greater in the intact membranes compared to their liposomes, indicating greater fluidity in the liposomes. Compositional studies suggested that the high fluidity of this membrane was due to its low ratios of protein/lipid (w/w), cholesterol/phospholipid (mol/mol), and sphingomyelin/phosphatidylcholine (mol/mol).
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PMID:Isolation and partial characterization of basolateral membranes from rat proximal colonic epithelial cells. 683 Jul 71


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