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  • Book
    Lipid Metabolism Branch, Division of Heart and Vascular Diseases, National Heart, Lung, and Blood Institute.
    Contents:

    v. 1. The prevalence study, aggregate distribution of lipids, lipoproteins and selected variables in 11 North American populations.
    Digital Access Google Books 1980-
    Print Access Request
    Location
    Version
    Call Number
    Items
    Stored offsite. Please request print.
    1980-
    RC632.L5 L76
    1
  • Article
    van Dijk W, Maier H, van den Eijnden DH.
    Biochim Biophys Acta. 1976 Oct 22;444(3):816-34.
    The properties and subcellular distribution of CMP-N-acetylneuraminic acid (CMP-NAcNeu) hydrolase were studied in the cortex of calf kidney. The pH optimum was 9.0 in both Tris - HCl and glycine/NaOH buffer. The apparent Km was 0.47 mM and the apparent V 15.3 mumol/h/g wet wt of calf kidney cortex. A stimulation by divalent metal ions (Ca2+ and Mg2+) was demonstrated for the hydrolase. In the presence of Triton X-100 an increase in enzyme activity was observed. CMP-NAcNeu hydrolase was inhibited by EDTA, beta-mercaptoethanol, nucleoside phosphates and nucleotide-sugars. The inhibition was more pronounced when a sub-optimal CMP-NAcNeu concentration was used. The enzyme appeared to be localized in the plasma membranes. In the plasma membrane preparation of calf kidney cortex, which was derived mainly from the proximal tubule cells, the yield of CMP-NAcNeu hydrolase (13%) and its increase in specific activity (9-fold) was as high as for the plasma membrane marker enzymes. From subcellular distribution studies it appeared that the enzyme was localized mainly at the bursh border side of the plasma membrane of the proximal tubule cell.
    Digital Access Access Options