Published 1990 .
Written in EnglishRead online
|Statement||by Taha A. Kumosani|
|The Physical Object|
|Pagination||ix, 129 leaves :|
|Number of Pages||129|
Download Characterization and partial purification of the plasma membrane ATPase of Rhodotorula glutinis
In this report, a first attempt at solubilization and purification of the ATPase from the plasma membrane of the yeast Rhodotorula glutinis is described. Start-ing with a pure, homogenous preparation of the plasma membrane which is free from any ATPase contamination from intracellular organelles, a successful sol.
The pH optimum of the plasma membrane ATPase isas compared with for the mitochondrial ATPase. In addition to oligomycin, the enzyme is not sensitive to other inhibitors of the mitochondria) ATPase as azide, dicyclohexylcarbodiimide and the mitochondrial ATPase inhibitor by: The optimal conditions for solubilization of the ATPase ac- tivity from the plasma membrane of Rhodotorula glutinis by zwitter- ionic detergent Z were found to be: mg/ml (5X cmc) of Z- 3.
The K +-stimulated ATPase was partially purified from a plasma membrane fraction of suspension cultured cells of rose (Rosa damascena) by two different solubilization procedures.
Solubilization with 30 m m octyl-β- d -glucopyranoside followed by precipitation with ammonium sulfate increased the specific activity of the enzyme about by: plasma membrane marker enzymes.
Treatment of the plasma membrane fraction with M KCI removes some protein and activity of granule enzymes, leading to an about fold enrichment in specific activity of plasma membrane marker enzymes.
In particular, there is a fold enrichment in a Ca2+-dependentCited by: Summary. Characteristics of the native and reconstituted H +-ATPase from the plasma membrane of red beet (Beta vulgaris L.) were examined. The partially purified, reconstituted H +-ATPase retained characteristics similar to those of the native plasma membrane H +-ATPase following reconstitution into activity and H + transport of both enzymes were inhibited by vanadate.
Abstract. The plasma membrane ATPase of mung bean (Phaseolus mungo L.) roots has been solubilized with a two-step procedure using the anionic detergent, deoxycholate (DOC) and the zwitterionic detergent, zwittergent as follows: (a) loosely bound membrane proteins are removed by treatment with % DOC; (b) The ATPase is solubilized with % zwittergent in the presence of 1%.
Abstract. The phosphorylated protein associated with a deoxycholate-extracted plasma membrane fraction from corn (Zea mays L. var WF9 × Mol7) roots was characterized in order to correlate its properties with those of plasma membrane phosphorylation, like that of plasma membrane ATPase, was dependent on Mg 2+, substrate specific for ATP, insensitive to azide, oligomycin, or.
Kasamo K () Reconstitution and characterization of H-translocating ATPase from the plasma membrane of Phaseolus mungo L. roots. Plant Cell Physiol 19–28 Google Scholar Kasamo K, Nouchi I () The role of phospholipids in plasma membrane ATPase activity in Vigna radiata L.
(mung bean) roots and hypocotyls. Characterization of Plasma Membrane Proteins in Mammalian Kidney dependent ATPase purification method of Nakao el al. (12). The membrane suspension (about 5 mg per ml) was mixed with half of its volume of a solution of 6 M NaI, M Tris-HCl buffer, pHand 15 mM EDTA.
Vara F, Serrano R () Partial purification and properties of the protontranslocating ATPase of plant plasma membranes. J Biol Chem – PubMed Google Scholar Vara F, Serrano R () Phosphorylated intermediate of the ATPase of plant plasma membranes.
Dupont FM, Leonard RT. Solubilization and partial purification of the adenosine triphosphatase from a corn root plasma membrane fraction. Plant Physiol. May; 65 (5)– [PMC free article] Fairbanks G, Steck TL, Wallach DF. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
Biochemistry. Within the last six years, this ATPase has been characterized in a number of cultivated plant species, especially in crops and beet cultivars.
Reports on characterization of the plasma membrane ATPase in wild plant species. that have not been bred for high nutrient uptake. are scarce (Yoshida er aI.• on Dactylis glomerata. Partial purification methods involve separation of membrane fragments by differential centrifugation (Skou, ) density gradient centrifugation (Emmelot and Bos, ) treatment with sodium deoxycholate (Skou, ) or treatment with NaI (Nakao et al., ) which appears to decrease the amount of ouabain-insensitive ATPase.
Abstract. We have characterized the respiratory system of the aerobic actinomycete Nonomuraea sp. ATCC The plasma membrane of the microorganism is shown to contain a protonmotive respiratory chain and H + respiratory chain is made up of a rotenone-sensitive NADH-quinone oxidoreductase, a four subunits aa 3-type cytochrome c oxidase and a bc 1 complex.
The plasma membrane fractions have a density in sucrose of and The yield is to mg per g of corpus luteum.
This fraction is char- acterized by electron microscopy, enzymatic assay, and binding properties of lzluteinizing hormone.
The plasma membrane fraction is free of nuclei and mito. This paper describes partial purification and characterization of a vanadate-sensitive H+-ATPase from plasma membranes of Dunaliella acidophila, an extremely acidophilic unicellular alga (I.
Sekler, H.U. Glaser, U. Pick  J Membr Biol 51–57). Purification is based on the insolubility in and stability of the enzyme in Triton X The yeast (Zygosaccharomyces rouxii) contains a plasma membrane ATPase which exhibits some properties similar to those of the Na + /K +-activated Mg 2+-dependent ATPases hitherto reported as existing almost exclusively in animal of Z.
rouxii grown under low salt conditions and adapted to media containing 18% NaCl have Mg 2+-dependent ATPase activity which. The plasma membrane H +-ATPase kDa protein generates a protonmotive force (PMF). PMF consists of a membrane potential and a pH gradient, which have separate roles.
• H +-ATPase phosphorylation regulates solute transport and cell expansion. A handful of different phosphosites have opposing effects on pump activity.
The plant plasma membrane H +-ATPase (PMA) creates a proton electrochemical gradient across the membrane, providing a driving force for ion and metabolite transport by a large range of secondary transporters (for reviews, see refs. 1 and 2). Although H +-ATPases consist of a single type of polypeptide, in some cases, they exist as homooligomers.
A Na+ -ATPase was partially purified from plasma membranes of the marine alga Heterosigma akashiwo. The plasma membranes of H. akashiwo cells were collected by differential centrifugation with subsequent discontinuous gradient centrifugation. Na+ -ATPase activity was associated with the resultant plasma membrane fraction and was stimulated to the greatest extent in the presence of to Purification and Characterization of the Pigments from Rhodotorula glutinis DFR-PDY Isolated from Natural Source 12B.V.
Latha and K. Jeevaratnam 1Microbiology Discipline, Defence Food Research Laboratory, Siddarthanagar, MysoreIndia 2Department of Biochemistry and Molecular Biology, Pondicherry University Kalapet, Puducherry Purification ofthe ATPase. A35,gpellet was used as the source ofplasma membranes since it has been shown that this fraction is more highly enriched in plasma membranes than is g microsomal pellet (21).
Rather than attempting to purifythe plasmamembranesfurther, wechosesimplyto purify the ATPase directly from this crude membrane. Partial characterization of the plasma membrane ATPase from arho 0 petite strain ofSaccharomyces cerevisiae.
Journal of Bioenergetics and Biomembranes12 (), DOI: /BF Gabriel M. Umezurike, Anya O. Anya. Kinetic analysis of the purified ATPase showed a K M value for ATP in the presence of Mg 2+ of mM and a V max of 10 U mg −1 protein at pH at 37°C ().The inhibitory effect of azide was further studied, and was found to be a mixed non-competitive inhibitor with a K I of mM ().It has been hypothesized that the negatively charged azide ion binds via the positive charge of Mg 2+ to.
Bowman BJ, Slayman CW. Characterization of plasma membrane adenosine triphosphatase of Neurospora crassa. J Biol Chem. May 25; (10)– Cantley LC, Jr, Josephson L, Warner R, Yanagisawa M, Lechene C, Guidotti G. Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.
The phosphorylation of the plasma membrane H +-ATPase and interaction with the proteins (5) were enhanced by the application of Mg and/or IAA (6) under Al stress, resulting in activation of.
Purification of Plasma Membrane ATPase Unless otherwise indicated, a11 operations were canied out at O to 4OC. Crude plasma membrane vesicles containing to 6 mg of protein/mL (30 mL) were mixed with 90 mL of extraction buffer containing 20 m~ Tris-Hepes, pH 7, 10% SUC; 2 mM EDTA, 1 mM DTT, and the protease inhibitors.
was similar to that found in liver plasma membranes. Phosphodiesterase, acid phosphatase and ATPase were purified 8- 4- and 2-fold, respectively, in the membrane fractions, whereas succinic dehydrogenase, esterase, and a variety of P-glycosidases were present only at very low levels.
The plasma‐membrane‐associated ATPase of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius characterized in a previous work [M. Lübben & G. Schäfer () Eur. Biochem.–] has been can be easily removed from the membrane by mild treatment with zwitterionic detergents, therefore it appears to be a peripheral membrane protein analogous to the.
The plasma membrane Ca 2+ ATPase (PMCA) 1 pumps Ca 2+ out of the cell, reducing its concentration in the cytosol to the level compatible with the messenger function ().In excitable tissues, e.g.
heart, it does so in concert with the Na + /Ca 2+ exchanger ().The pump has been detected in all mammalian cells studied so far (1, 3), although differences in the level of its expression have been.
Candida albicans is an opportunistic fungal pathogen of humans. Treatment of C. albicans infections relies on azoles, which target the lanosterol 14α-demethylase (Erg11p) encoded by the ERG11 gene.
Our results show that targeted gene disruption of ERG11 can result in resistance to ergosterol-dependent drugs (azoles and amphotericin B), auxotrophy and aerobically viable erg11Δ/Δ cells. The NeurosporacrassaH -ATPase is active as a monomer but can form stable hexamers in the plasma membrane under certain conditions (6).
Cryoelectron microscopy studies of this H - ATPase reconstituted into 2D crystals (7) or in detergent (8) also showed a hexamer. The quaternary structure of the H -ATPase might also de. The carboxyl terminus of yeast plasma membrane H(+)-ATPase is an autoinhibitory domain, and its effect is counteracted by modification of the enzyme triggered by glucose metabolism (Portillo, F.
Ahlers J, Ahr E, Seyfarth A () Kinetic characterization of plasma membrane ATPase from Saccharomyces cerevisiae. Mol Cell Biochem 39–49 PubMed CrossRef Google Scholar Amanuma H, Hoh J, Anraku Y () Proton-dependent binding of proline to carrier in Escherichia coli membrane.
Substitution of nucleoside triphosphates for ascorbate in the thymine 7-hydroxylase reaction of Rhodotorula glutinis. L M Wondrack, B J Warn, M D Saewert, and M T Partial purification of the factors required for the initiation of protein synthesis in wheat germ.
Lymphocyte and erythrocyte plasma membrane glycoproteins as inhibitors of. were used for the isolation and purification of dalton protein. Purification of chlamydiae.
Chlamydiae were harvested from HeLa cell monolayers grown in cm2polystyrene culture flasks (CorningGlassWorks, Corning, N.Y.), with % of the cells containing inclusionsat48hpostinoculation. Mediumwaspoured off, andcellswereremovedwith4.
Structure and Function of Plasma Membrane ATPase. ROS sensors such as membrane-localized histidine kinases can sense extracellular and intracellular ROS.
pathogen attack or (b) abiotic stress. Upon pathogen attack, receptor-induced signaling activates plasma membrane or apoplast-localized oxidase Mechanisms of Salinity Tolerance. Partially (6-fold) purified plasma membrane ATPase from an ethanol-sensitive yeast, Kloeckera apiculata, had an optimum pH ofan optimum temperature of 35°C, a.
Friedrich FENZL, Michael DECKER, Dieter HAASS, Widmar TANNER, Characterization and Partial Purification of an Inducible Protein Related to Hexose Proton Cotransport of Chlorella vulgaris, European Journal of Biochemistry, /jtbx, 72, 3, (), (). The translocase of the outer mitochondrial membrane (TOM) complex is a preprotein translocase that mediates transport of nuclear-encoded mitochondrial proteins across the outer mitochondrial membrane.
Here we report the purification of this protein complex from Arabidopsis. On blue-native gels the Arabidopsis TOM complex runs at kD and can be dissected into subunits of 34, 23, 21, 8, 7.Click on the article title to read more.Isolation, Partial Purification and Characterization of Phospholipid Hydroperoxide Glutathione Peroxidase (Phgpx Enzyme from Oryza Sativa Seedlings Om Prakash Verma 1*, Pankaj Kumar Ojha, Shashi B Bailey1, Pankaj Singh1, Rajendra Dubey2 and 3 1Jacob School of Biotechnology & Bioengineering, SHIATS, Allahabad 2Galaxy Concepts Kolkata.