Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The F1 portion of H(+)-translocating ATPase as purified from membrane vesicles of Vibrio parahaemolyticus by a rapid procedure. The whole purification process (from culture of cells to purification of the enzyme) could be completed in 1 day. The F1-ATPase consists of five subunits (alpha, beta, gamma, delta and epsilon) like F1 of Escherichia coli and other microorganisms. The F1-ATPase of V. parahaemolyticus showed some interesting properties. Its activity was greatly stimulated by high concentrations (about 0.5 M) of SO4(2-), SO3(2-) and CH3COO-, their effects decreasing in this order. Among the anions tested, Cl- and NO3- were ineffective, or rather inhibitory, and cations had no significant effects. Ethanol (or methanol) stimulated the activity 2- to 3-fold. The activity was inhibited by 4-acetamido-4'-isothiocyanostilbene 2,2'-disulfonate (SITS) (an anion exchanger inhibitor), tetrachlorosalicylanilide (TCS) (an H+ conductor), azide and N-ethylmaleimide. Zinc inhibited the activity only slightly, although it strongly inhibited the ATPase activity in membrane vesicles.
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PMID:Rapid purification and characterization of F1-ATPase of Vibrio parahaemolyticus. 214 93

Several mutants of yeast lacking the porin gene have been found stable and viable on glucose or glycerol media. Ethanol-supported respiration of porin-free mutant and wild cells appeared equally coupled in vivo being similarly depressed by inhibitors of ADP/ATP translocase or of ATP synthase and stimulated by the uncoupler FCCP. The absence of porin in isolated mutant mitochondria hardly impaired the electron flux but increased the requirement for Mg2+ (or Ca2+) and for ADP and carboxyatractylate concentrations necessary to drive effectively state 3 - state 4 and state 4 - state 3 transitions, respectively. The existence of another porin species, possibly controlled by bivalent cations, is postulated.
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PMID:The respiration of cells and mitochondria of porin deficient yeast mutants is coupled. 216 77

Previous attempts to isolate a stable F0F1-ATPase complex (H(+)-translocating ATPase) from Vibrio parahaemolyticus have been unsuccessful. Using new non-ionic detergents (alkyl thiomaltosides), a stable F0F1 complex with a high specific activity (15-25 units/mg protein) was purified and characterized. The purified F0F1-ATPase consists of eight subunits (alpha, beta, gamma, delta, epsilon, a, b and c). The new detergents, in combination with sucrose (or glycerol), lipid, dithiothreitol and phenylmethylsulfonyl fluoride, effectively stabilized the F0F1 complex. The ATPase activity of the F0F1 complex was greatly increased by anions, such as SO4(2-) and SO3(2-). Sodium ion increased the activity by about 2-fold. Dicyclohexylcarbodiimide, Zn2+, 4-acetamido-4'-isothiocyanostilben-2,2'disulfonate and tetrachlorosalicylanilide inhibited F0F1-ATPase activity. Ethanol, which stimulated F1-ATPase activity, inhibited F0F1-ATPase activity. Methanol, Na3VO4 and bafilomycin A1 did not have any significant effect on F0F1-ATPase activity, although methanol, like ethanol, stimulated F1-ATPase activity.
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PMID:F0F1-ATPase of Vibrio parahaemolyticus: purification using new detergents and characterization. 794 6

Cultured mouse heart-derived myocardial and non-muscle cells were exposed to ethanol, stained with cell-permeant fluorescent vital probes, JC-1 (5,5',6,6'-tetrachloro-1,1',3,3'-tetraethylbenzimidazolyl-carbocyanine iodide) and oxidation-sensitive dihydrorhodamine 123, and analyzed by flow cytometry to elucidate ethanol-induced time-wise alterations in the mitochondrial membrane potential (DeltaPsim) and the production of reactive oxygen species (ROS). Ethanol (50 and 200 mM) not only hyperpolarized DeltaPsim of both types of cells but also dose-dependently increased ROS production at 24 h, although a 200-mM dose reduced the production until 3 h. These cell pathophysiological reactions suggest the depression of mitochondrial ATPase and mitochondrial respiratory chain. However, differences between these cells appeared after a 24-h exposure to 200 mM ethanol: the increase in ROS production was approximately twice as large for myocardial cells as for non-muscle cells; and the side-scatter parameter of light scattering significantly increased for myocardial cells, but not for non-muscle cells. All these myocyte-specific alterations indicate an increase in the mitochondrial fraction in a cell. This reaction might be a countermeasure against ethanol-induced dysfunction of mitochondrial respiration that is needed to meet the energy requirements of spontaneous myocardial contractions.
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PMID:Ethanol hyperpolarizes mitochondrial membrane potential and increases mitochondrial fraction in cultured mouse myocardial cells. 1647 59