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  • Book
    edited by Sumitra Deb, Swati Palit Deb.
    Contents:
    Detecting and quantifying p53 isoforms at mRNA level in cell lines and tissues / Marie P. Khoury ... [et al.]
    Detecting p53 isoforms at protein level / Virginie Marcel ... [et al.]
    Autophagy, senescence, and apoptosis / Rachel W. Goehe ... [et al.]
    p53 and cell cycle effects after DNA damage / Emir Senturk and James J. Manfredi
    p53 ubiquitination and proteasomal degradation / Ian M. Love, Dingding Shi, and Steven R. Grossman
    Identification of p53 in mitochondria / Angelina V. Vaseva and Ute M. Moll
    Identification of novel mutant p53 interacting proteins by proteomic analysis / Sumitra Deb and Paul R. Graves
    Identification of small molecules affecting p53-MDM2/MDMX interaction by fluorescence polarization / Qi Zhang and Hua Lu
    Determine the effect of p53 on chemosensitivity / Emir Senturk and James J. Manfredi
    Measurement of chemosensitivity and growth rate in p53 expressing cells / Mahesh Ramamoorthy ... [et al.]
    Mutant p53 in cell adhesion and motility / W. Andrew Yeudall, Katharine H. Wrighton, and Sumitra Deb
    Use of the DNA fiber spreading technique to detect the effects of mutant p53 on DNA replication / Rebecca A. Frum, Sumitra Deb, and Swati Palit Deb
    Generation of p53-deficient induced pluripotent stem cells from mouse embryo fibroblasts / Evguenia M. Alexandrova and Ute M. Moll
    p53 actions on microRNA expression and maturation pathway / Hiroshi I. Suzuki and Kohei Miyazono
    Isolation and characterization of murine multipotent lung stem cells / Venkat S. Gadepalli, Catherine Vaughan, and Raj R. Rao
    Generation of p53 knock-down cell lines / Catherine Vaughan, Swati Palit Deb, and Sumitra Deb
    ChIP for identification of p53 responsive DNA promoters / Jun-Ming Liao and Hua Lu
    ChIP-on-chip to identify mutant p53 targets / Frauke Goeman, Giulia Fontemaggi, and Giovanni Blandino
    ChIP sequencing to identify p53 targets / Catherine Vaughan, Brad Windle, and Sumitra Deb.
    Digital Access Springer 2013
  • Article
    Leger C, Bauchart D, Flanzy J.
    Comp Biochem Physiol B. 1977;57(4):359-63.
    1. The Michaelis constant (Km) of the trout pancreatic lipase is 1.3 x 10(-6) M tributyrin, calculated by the interface concentration of the emulsion. This value is lower than that of porcine pancreatic lipase. 2. The lipase hydrolyses tributyrin in a Ca2+ free medium. Conversely, Ca2+ is essential for the lipolysis of triolein. The cation might be an effector of the reaction, but it seems to remove the inhibition of the enzyme by its product. 3. The curves of the lipase activity according to bile salt concentration seem to suggest the existence of a colipase, that we have not evidenced yet by direct procedures. 4. The apparent molecular weight of the lipase seems to be lower in the trout than in the species studied so far.
    Digital Access Access Options