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  • GTP  (1)
  • artificial neural network  (1)
  • binding activity  (1)
  • 1990-1994  (3)
  • 1
    ISSN: 1572-8773
    Keywords: binding activity ; ferric citrate binding protein ; FPLC chromatofocusing ; iron uptake ; purification of membrane protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In our earlier paper, it was demonstrated that the FecA receptor protein from Escherichia coli UT5600/pBB2 (leu −, proC −, trpE −, entA −, rpsl −, Δ(ompT-fepA)−/Ampr, fepA) binds with ferric enterobactin. In order to explore this further the outer membrane receptor protein, FecA, has been isolated from UT5600 (fepA −) and purified to homogeneity by DE-52-cellulose anion exchange chromatography followed by MonoPFPLC chromatofocusing. Partially purified FecA and homogeneous FecA show binding activity to [55Fe]ferric enterobactin and the binding is specific. Binding activity of FecA can be enhanced by ferric citrate. Lipopolysaccharide-free FecA as ascertained by silver staining and the endotoxin test still retains the same activity. In vivo uptake studies using different strains of E. coli suggest that FecA in E. coli plays an important role in ferrienterobactin transport.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Microchimica acta 111 (1993), S. 199-206 
    ISSN: 1436-5073
    Keywords: chemometrics ; artificial neural network ; multi-component calibration ; potentiometric acid-base titration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A three-layer artificial neural network model with back-propagation of error is used to treat potentiometric acid-base titration data for estimating the concentrations of individual components in polybasic weak acid mixtures. The network's architecture and parameters were optimized and an empirical rule for dynamically adjusting the learning rate is put forward to improve the network's performance. Satisfactory prediction results were obtained for three-component samples containing maleic acid, propandioic acid and succinic acid with an average relative error of 4.5%.
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  • 3
    ISSN: 1573-5028
    Keywords: ATP ; GTP ; protein kinase ; receptor ; rice ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A receptor-like protein kinase, OsPK10, has been cloned from rice (Oryza sativa). The 2.8 kb cDNA contains an open reading frame capable of encoding a peptide sequence of 824 amino acids. The topological features of the predicted OsPK10 protein include an N-terminal signal peptide, a cysteine-rich extracellular ligand-binding domain, a membrane-spanning segment, and a cytoplasmic domain possessing all the hallmarks of catalytic domains of eukaryotic protein kinases. The cytoplasmic domain was selectively expressed in Escherichia coli and assayed for kinase activity. The results show the protein is capable of autophosphorylation using either ATP or GTP as the phosphate donor. Phosphoamino acid analysis reveals phosphorylation of threonines, consistent with the substrate specificity indicated by sequence motifs in the catalytic core. A single amino acid substitution of Glu for Lys-528 completely abolishes autophosphorylation activity. DNA gel blot analyses suggest that the haploid rice genome contains a single copy of the OsPK10 gene. OsPK10 transcripts appear to be more abundant in shoots than in roots of rice seedlings.
    Type of Medium: Electronic Resource
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