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    PURIFICATION AND CHARACTERIZATION OF BOVINE LIVER ORNITHINE DECARBOXYLASE

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    Author
    Haddox, Mari Kristine
    Issue Date
    1980
    Keywords
    Enzymes -- Purification.
    Ornithine decarboxylase.
    Advisor
    Russell, Diane
    
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    Show full item record
    Publisher
    The University of Arizona.
    Rights
    Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
    Abstract
    Ornithine decarboxylase has been purified to apparent homogeneity from thioacetamide-stimulated calf liver. The purification process, which has been developed to circumvent the lability of the enzyme, employs ion exchange chromatography, gel filtration, hydroxylapatite chromatography, non-denaturing gel electrophoresis, and sulfhydryl affinity chromatography. The enzyme is purified 71,500-fold to a final specific activity of 286,000 pmol/min/mg protein. Non-denaturing gel electrophoresis indicates a single protein present in the final preparation. The enzyme has a Stokes radius of 3.14 nm as indicated by gel filtration and a monomeric molecular weight of 52,000 daltons as indicated by denaturing gel electrophoresis. The K(m) values for ornithine and pyridoxal phosphate are 0.16 mM and 2.5 μM, respectively. Putrescine inhibits the enzyme (Kᵢ 10mM). The existence of three ionic forms of ornithine decarboxylase is suggested by fractionation of the preparation by gradient sievorptive chromatography. Mammalian ornithine decarboxylase is apparently a metalloenzyme. A variety of structurally distinct metal chelators inhibit the enzyme. A non-chelating analog of the most potent chelator, 1,10-phenanthroline, is without effect. The order of efficacy of the chelators suggests the involvement of a metal from the transition series. Incubation of the enzyme with charcoal or Cibacron Blue-Agarose results in a loss of catalytic activity suggesting that the ornithine decarboxylase may also contain a bound nucleotide.
    Type
    text
    Dissertation-Reproduction (electronic)
    Degree Name
    Ph.D.
    Degree Level
    doctoral
    Degree Program
    Graduate College
    Microbiology
    Degree Grantor
    University of Arizona
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