399 research outputs found
A Method Of Distinguishing Between Aspartic Acid And Asparagine And Between Glutamic Acid And Glutamine During Sequence Analysis By The Dansyl-edman Procedure
No full textFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)[No abstract available]5021551582009/10554-8; FAPESP; Conselho Nacional de Desenvolvimento Científico e Tecnológico; 2011/11171-5; FAPESP; Conselho Nacional de Desenvolvimento Científico e Tecnológico; 306580/2012-8; CNPq; Conselho Nacional de Desenvolvimento Científico e Tecnológico; 484254/2012-0; CNPq; Conselho Nacional de Desenvolvimento Científico e TecnológicoFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Gray, (1967) Methods Enzymol., 11, p. 469Hartley, (1970) Biochem. J., 119, p. 805Offord, (1966) Nature (London), 211, p. 591Rosenthal, Atassi, (1967) Biochim. Biophys. Acta, 147, p. 410Atassi, Rosenthal, (1969) Biochem. J., 111, p. 593Brown, Subba, (1960) J. Amer. Chem. Soc., 82, p. 681Brown, Korytnyk, (1960) J. Amer. Chem. Soc., 82, p. 3866Brown, Heim, (1964) J. Amer. Chem. Soc., 86, p. 3566Riva, Barra, Bossa, Carloni, Fasella, Doonan, Doonan, Walker, (1974) Atti Accad. Naz. Lincei Rend., , in the pressDoonan, Doonan, Riva, Vernon, Walker, Bossa, Barra, Fasella, (1972) Biochem. J., 130, p. 443Bossa, Barra, Carloni, Fasella, Riva, Doonan, Doonan, Walker, The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase. (1973) Biochem J, 133, p. 805Habermann, Jentsch, (1967) Hoppe-Seylers Z. Physiol. Chem., 348, p. 37Billingham, Morley, Hanson, Shipolini, Vemon, (1973) Nature (London), 245, p. 163Woods, Wang, Separation of dansyl-amino acids by polyamide layer chromatography (1967) Biochimica et Biophysica Acta (BBA) - Protein Structure, 333, p. 369Crowshaw, Jessup, Ramwell, (1967) Biochem. J., 103, p. 79Airoldi, L.P. da S. and Doonan, S. Unpublished workOvchinnikov, Egorov, Aldanova, Feigina, Lipkin, Abulaev, Grishin, Nosikov, (1973) FEBS Lett., 29, p. 3
Primary structure of aspartate aminotrasferase from horse hearth and comparison with that of other homotopic and heterotopic isoenzymes
No full textSulphydryl groups of mitochondrial aspartate aminotransferase from horse heart were titrated with 5,5'-dithiobis (2-nitrobenzoic acid). From analysis of peptic peptides, 378 amino acid residues (94.3% of the total) in the protein were identified. The results of amino acid sequence analysis are compared with those of cytosolic and mitochondrial aspartate aminotransferases from other source
Partial amino-acid sequence and cysteine reactivities of cytosolic aspartate aminotrasferase from horse heart
No full textThe amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cerevisiae).
No full textThe amino acid sequence of cytosolic aspartate aminotransferase from human liver
No full text1. The cytosolic aspartate aminotransferase was purified from human liver. 2. The isoenzyme contains four cysteine residues, only one of which reacts with 5,5'-dithiobis-(2-nitrobenzoic acid) in the absence of denaturing agents. 3. The amino acid sequence of the isoenzyme is reported, as determined from peptides produced by digestion with trypsin and with CNBr, and from sub-digestion of some of these peptides with Staphylococcus aureus V8 proteinase. 4. The isoenzyme shares 48% identity of amino acid sequence with the mitochondrial form from human heart. 5. Comparisons of the amino acid sequences of all known mammalian cytosolic aspartate aminotransferases and of the same set of mitochondrial isoenzymes are reported. The results indicate that the cytosolic isoenzymes have evolved at about 1.3 times the rate of the mitochondrial forms. 6. The time elapsed since the cytosolic and mitochondrial isoenzymes diverged from a common ancestral protein is estimated to be 860 x 10(6) years. 7. Experimental details and confirmatory data for the results presented here are given in a supplementary paper that has been deposited as a Supplementary Publication SUP 50158 (25 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1990) 265, 5
Uptake of aspartate aminotransferase into mitochondria in vitro causes efflux of malate dehydrogenase and vice versa
No full textStructure of the active site of sulfite dehydrogenase from Starkeya novella
No full textIn this paper, we report the results of molybdenum K-edge X-ray absorption studies performed on the oxidized and reduced active sites of the sulfite dehydrogenase from Starkeya novella. Our results provide the first direct structural information on the active site of the oxidized form of this enzyme and confirm the conclusions derived from protein crystallography that the molybdenum coordination is analogous to that of the sulfite oxidases. The molybdenum atom of the oxidized enzyme is bound by two Mo=O ligands at 1.73 A and three thiolate Mo-S ligands at 2.42 A, whereas the reduced enzyme has one oxo at 1.74 A, one long oxygen at 2.19 A (characteristic of Mo-OH2), and three Mo-S ligands at 2.40 A.Christian J. Doonan, Ulrike Kappler and Graham N. Georg
Inorganic molecular toxicology and chelation therapy of heavy metals and metalloids
No full textGraham N. George, Ingrid J. Pickering, Christian J. Doonan, Malgorzata Korbas, Satya P. Singh and Ruth E. Hoffmeye
Perturbation of cytokinin and ethylene-signalling pathways explain the strong rooting phenotype exhibited by Arabidopsis expressing the Schizosaccharomyces pombe mitotic inducer, cdc25
No full textBackground
Entry into mitosis is regulated by cyclin dependent kinases that in turn are phosphoregulated. In most eukaryotes, phosphoregulation is through WEE1 kinase and CDC25 phosphatase. In higher plants a homologous CDC25 gene is unconfirmed and hence the mitotic inducer Schizosaccharomyces pombe (Sp) cdc25 has been used as a tool in transgenic plants to probe cell cycle function. Expression of Spcdc25 in tobacco BY-2 cells accelerates entry into mitosis and depletes cytokinins; in whole plants it stimulates lateral root production. Here we show, for the first time, that alterations to cytokinin and ethylene signaling explain the rooting phenotype elicited by Spcdc25 expression in Arabidopsis.
Results
Expressing Spcdc25 in Arabidopsis results in increased formation of lateral and adventitious roots, a reduction of primary root width and more isodiametric cells in the root apical meristem (RAM) compared with wild type. Furthermore it stimulates root morphogenesis from hypocotyls when cultured on two way grids of increasing auxin and cytokinin concentrations. Microarray analysis of seedling roots expressing Spcdc25 reveals that expression of 167 genes is changed by > 2-fold. As well as genes related to stress responses and defence, these include 19 genes related to transcriptional regulation and signaling. Amongst these was the up-regulation of genes associated with ethylene synthesis and signaling. Seedlings expressing Spcdc25 produced 2-fold more ethylene than WT and exhibited a significant reduction in hypocotyl length both in darkness or when exposed to 10 ppm ethylene. Furthermore in Spcdc25 expressing plants, the cytokinin receptor AHK3 was down-regulated, and endogenous levels of iPA were reduced whereas endogeous IAA concentrations in the roots increased.
Conclusions
We suggest that the reduction in root width and change to a more isodiametric cell phenotype in the RAM in Spcdc25 expressing plants is a response to ethylene over-production. The increased rooting phenotype in Spcdc25 expressing plants is due to an increase in the ratio of endogenous auxin to cytokinin that is known to stimulate an increased rate of lateral root production. Overall, our data reveal important cross talk between cell division and plant growth regulators leading to developmental changes
A 3-D diamondoid MOF catalyst based on in situ generated [Cu(L)2] N-heterocyclic carbene (NHC) linkers: hydroboration of CO(2)
No full textIncludes supplementary informationA new MOF, [Zn4O{Cu(L)2}2] (1), with a 4-fold interpenetrated 3D diamondoid structure was synthesised from in situ generated [Cu(L)2] NHC linkers. MOF 1 possesses tetrahedral Zn4O nodes, which are unusually coordinated by four pairs of carboxylates from four [Cu(L)2] linkers, and 14 A 1-D pore channels lined with [Cu(L)2] moieties that catalyse the hydroboration of CO2.Alexandre Burgun, Rachel S. Crees, Marcus L. Cole, Christian J. Doonan and Christopher J. Sumb
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