Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Gossypol acetic acid was given to male rats at a dose of 7.5 mg/rat/day six days a week for ten weeks. After nine weeks of gossypol treatment no implantation sites were observed in the females mated with gossypol treated males. After ten weeks of gossypol treatment all the spermatozoa in the vas deferens were non-motile. Gossypol treatment did not affect the body weight and the weights of the accessory sex organs. Plasma LH and FSH levels, hCG binding in testis and succinic dehydrogenase (SDH) and adenosine triphosphatase (ATPase) activities in liver, kidney and testis were not affected by gossypol treatment. Histological observations of the testis revealed partial damage to the seminiferous tubules. Single high doses of gossypol did not induce significant changes in the body weight and weights of testis and accessory sex organs. ATPase activity in the testis was reduced significantly after gossypol treatment, the enzyme activity in liver and kidney, was however, affected at high doses only. Gossypol treatment had no effect on the histoarchitecture of the testis. Intratesticular administration of gossypol evoked localized damage in the testis. Gossypol treatment had no effect on I125 FSH binding to the rat testis homogenate in vitro.
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PMID:Studies on the male antifertility agent--gossypol acetic acid. V. Effect of gossypol acetic acid on the fertility of male rats. 716 22

Isatin (10 microM) strongly inhibited the activity of rat brain monoamine oxidase-B (MAO-B) in vitro. At millimolar concentrations (1-10 mM) it inhibited brain acetylcholinesterase (AChE) and sodium, potassium-adenosine triphosphatase (Na+, K(+)-ATPase) activity also. However, isatin did not affect these enzymes after both acute and chronic treatments in vivo. Administration of isatin to rats at 300 mg/kg body weight for 2 and 6 h significantly raised brain serotonin levels. Chronic treatment for 20 days resulted in enhanced brain glycolipids and plasmalogen levels. There was no change in the levels of 5-hydroxy indole acetic acid (5 HIAA), phospholipids, cholesterol and gangliosides under these conditions.
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PMID:In vivo effects of isatin on certain enzymes, lipids & serotonergic system of rat brain. 782 61

Experiments were conducted to determine conditions essential for electrophoretic characterization of a detergent-extracted plasma membrane fraction from corn (Zea mays L.) roots. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) initially gave poor resolution of polypeptides in the plasma membrane fraction and, upon detergent treatment for purification of the proton-pumping adenosine triphosphatase (ATPase), showed no enrichment for a 100 kilodalton catalytic subunit characteristic of the ATPase. In contrast to SDS-PAGE, phenol urea acetic acid (PAU)-PAGE clearly resolved two polypeptides in the 100 kilodalton region that were enriched during detergent treatment and indicated at least one polypeptide forms a phosphorylated intermediate characteristic of the ATPase. Problems with SDS-PAGE were found to be caused, in part, by a combination of endogenous proteases and heat-induced aggregation of high molecular weight proteins. The usually standard procedure of boiling the sample prior to SDS-PAGE caused the aggregation of the 100 kilodalton polypeptides. By controlling for proteases using chymostatin and/or phenylmethane sulfonyl floride, and not boiling the sample prior to electrophoresis, two polypeptides were clearly resolved by SDS-PAGE in the 100 kilodalton region of Triton X-114-extracted membranes from corn, oat, barley, and tomato.
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PMID:Electrophoretic characterization of a detergent-treated plasma membrane fraction from corn roots. 1666 34

1. Tropomyosin preparations of the Bailey type, and those prepared in the presence of dithiothreitol to prevent oxidation of protein thiol groups, inhibit the Ca(2+)-activated adenosine triphosphatase (ATPase) of desensitized actomyosin by up to 60%. 2. The inhibitory activity of myofibrillar extracts and tropomyosin survives various agents known to denature proteins but to the action of which tropomyosin is unusually stable, namely heating at 100 degrees and mild tryptic digestion. It is destroyed by prolonged treatment with trypsin. 3. The ethylenedioxybis-(ethyleneamino)tetra-acetic acid (EGTA)-sensitizing factor present in extracts of natural actomyosin and myofibrils could be selectively destroyed, leaving unchanged the inhibitory effect on the Ca(2+)-activated ATPase. There was no correlation between the EGTA-sensitizing and the Ca(2+)-activated inhibitory activities of tropomyosin prepared under different conditions. 4. Optimum inhibition was achieved when tropomyosin and the myosin of desensitized actomyosin were present in approximately equimolar proportions. Tropomyosin had no effect on the Ca(2+)-activated ATPase of myosin measured under similar conditions. 5. Evidence is presented showing that the tropomyosin binds to desensitized actomyosin under the conditions in which the ATPase is inhibited.
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PMID:The effect of tropomyosin on the adenosine triphosphatase activity of desensitized actomyosin. 1674 51

The phosphorylated intermediate in the (Na + K)-activated adenosine triphosphatase (Na-K ATPase) has been characterized as an L-glutamyl-gamma-phosphate residue in the enzyme. This has been accomplished by digestion of the phosphorylated and nonphosphorylated forms of the enzyme with pepsin, reaction of the pepsin digests with [2,3-(3)H]N-(n-propyl)hydroxylmine, further digestion of the derivatized peptides with pronase in the presence of carrier L-glutamyl-gamma-N-(n-propyl)hydroxamate and carrier L-aspartyl-N-(n-propyl)hydroxamate, and chromatographic purification. An increment in radioactivity migrated with authentic L-glutamyl-gamma-N-(n-propyl)hydroxamate in a total of seven electrophoretic and chromatographic systems and on gel filtration. No increment in radioactivity was associated with authentic L-aspartyl-beta-N-(n-propyl)hydroxamate in five out of the seven chromatographic and electrophoretic systems. At the last stage of purification the radioactivity from the phosphorylated enzyme which migrated as L-glutamyl-gamma-N-(n-propyl)hydroxamate was 2(1/2) times that from the nonphosphorylated enzyme. On the basis of these results it is concluded that the phosphorylated intermediate in the Na-K ATPase is an L-glutamyl-gamma-phosphate residue. The beef brain Na-K ATPase has been solubilized with the nonionic detergent, Lubrol, and has been purified 10 times over that in the original microsomes. The soluble enzyme remains stable in the presence of ATP and either Na(+) or K(+). If the partially purified enzyme is electrophoresed in 3% polyacrylamide, followed by incubation with ATP, Na(+), K(+), and Mg(++), a single, somewhat diffuse, ATPase band, which is ouabain-sensitive is seen. Protein impurities are also seen on the gel. Gel electrophoresis, after treatment of the partially purified enzyme with phenol-acetic acid-urea, shows about 12 discrete protein bands. Studies on the site-directed alkylation of the (Na + K)-activated adenosine triphosphatase with haloacetate derivatives of cardiotonic steroids are reviewed. Efforts are now underway to specifically alkylate the cardiotonic steroid site of the Na-K ATPase with hellebrigenin 3-[2-(3)H]iodoacetate and to purify the subunit of the enzyme containing the cardiotonic steroid site by following radioactivity. Finally, a working model for the role of the Na-K ATPase in the coupled transport of Na and K is presented.
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PMID:On the molecular characterization of the sodium-potassium transport adenosine triphosphatase. 1987 52

The Gluconobacter phage GC1 is a novel member of the Tectiviridae family isolated from a juice sample collected during dry white wine making. The bacteriophage infects Gluconobacter cerinus, an acetic acid bacterium which represents a spoilage microorganism during wine making, mainly because it is able to produce ethyl alcohol and transform it into acetic acid. Transmission electron microscopy revealed tail-less icosahedral particles with a diameter of ~78 nm. The linear double-stranded DNA genome of GC1 (16,523 base pairs) contains terminal inverted repeats and carries 36 open reading frames, only a handful of which could be functionally annotated. These encode for the key proteins involved in DNA replication (protein-primed family B DNA polymerase) as well as in virion structure and assembly (major capsid protein, genome packaging ATPase (adenosine triphosphatase) and several minor capsid proteins). GC1 is the first tectivirus infecting an alphaproteobacterial host and is thus far the only temperate tectivirus of gram-negative bacteria. Based on distinctive sequence and life-style features, we propose that GC1 represents a new genus within the Tectiviridae, which we tentatively named "Gammatectivirus". Furthermore, GC1 helps to bridge the gap in the sequence space between alphatectiviruses and betatectiviruses.
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PMID:Bacteriophage GC1, a Novel Tectivirus Infecting Gluconobacter Cerinus, an Acetic Acid Bacterium Associated with Wine-Making. 2933 68


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