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  • Book
    edited by Anna S. Kashina.
    Contents:
    Protein arginylation: over 50 years of discovery / Anna S. Kashina
    Recollection of how we came across the protein modification with amino acids by aminoacyl trna-protein transferase / Hideko Kaji and Akira Kaji
    Arginyltransferase: a personal and historical perspective / Ricahrd L. Soffer
    Arginylation in a partially purified fraction of 150k x g supernatants of axoplasm and injured vertebrate nerves / Nicholas A. Ingoglia
    Preparation of ATE1 enzyme from native mammalian tissues / Anna S. Kashina
    Correlated measurement of endogenous ATE1 activity on native acceptor proteins in tissues and cultured cells to detect cellular aging / Hideko Kaji and Akira Kaji
    Assaying the posttranslational arginylation of proteins in cultured cells / Mauricio R. Galiano and Marta E. Hallak
    Assaying ATE1 activity in yeast by [beta]-Gal degradation / Anna S. Kashina
    Bacterial expression and purification of recombinant arginyltransferase (ATE1) and arg-tRNA synthetase (RRS) for arginylation assays / Junling Wang and Anna S. Kashina
    Assaying ATE1 activity in vitro/ Junling Wang and Anna S. Kashina
    High-throughput arginylation assay in microplate format / Sougata Sha, Junling Wang and Anna S. Kashina
    Assay of arginyltransferase activity by a fluorescent HPLC method / Koichi Takao
    Identification of arginylated proteins by mass spectrometry / Anna S. Kashina and Jon R. Yates III
    Analysis of arginylated peptides by subtractive edman degradation / Anna S. Kashina and Jon R. Yates III
    Transferase-mediated labeling of protein N-termini with click chemistry handles / Anne M. Wagner [and four others]
    Applying arginylation for bottom-up proteomics / H. Alexander Ebhardt
    Development of new tools for the studies of protein arginylation / Anna S. Kashina.
    Digital Access Springer 2015
  • Book
    volume editor, Walter Hayduk ; evaluators, Rubin Battino .. [et al.] ; compilers, M. Elizabeth Derrick ... [et al.].
    Summary: This volume contains numerical values and a critical analysis of solubility data for ethane in pure liquids, liquid mixtures, aqueous and organic solutions, and electrolytes, at both low and high pressures. For each published paper, an individual data sheet contains the experimental solubility, a description of the experimental apparatus, the purity of the materials used, and the experimental error where available. For each solute/solvent system the solubility data are critically assessed and recommended solubility values are presented. Nielsen 9780080262307 20160528

    Contents:
    (partial) Foreword. Preface. Introduction: The solubility of gases in liquids. Solubility of Ethane in the Following Solvents: Water. Mixed ethene-ethane gas in water at high pressure. Aqueous electrolyte solutions. Aqueous organic solutions. Alkanes. Non-polar solvents excluding alkanes. Alcohols. Polar solvents excluding water, aqueous solutions and alcohols. Various organic solvents and hydrogen sulfide at high pressure. System index. Registry number index. Author index. Nielsen 9780080262307 20160528
    Digital Access ScienceDirect, 1982
  • Article
    Chandrasena SI, Hird FJ.
    Comp Biochem Physiol B. 1978;61(2):191-4.
    1. The content of adenylic acid deaminase and of aspartate-2-oxoglutarate aminotransferase of skeletal muscle tissue from a variety of animals has been determined. 2. White (fast) muscle contained large amounts of adenylic acid deaminase and red (slow) muscle contained large amounts of aspartate aminotransferase. There was a general inverse relationship between the adenylic acid deaminase and the aspartate aminotransferase content of muscles from various vertebrates. Thus, there is no simple correlation between the capacity to produce inosinic acid and ammonia from adenylic acid and the capacity to catalyse the formation of aspartate for conversion of inosinic acid back to adenylic acid. 3. The absence of adenylic acid deaminase from the tail muscles of the yabbie and other invertebrates indicates a marked difference in the Animal Kingdom.
    Digital Access Access Options