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  • Title: Purification and some particular kinetic properties of rat spleen cytosolic deoxynucleotidase.
    Author: Fritzson P.
    Journal: Int J Biochem; 1991; 23(12):1403-9. PubMed ID: 1662163.
    Abstract:
    1. Rat spleen cytosolic deoxynucleotidase was purified 40,000-fold to almost homogeneity and had a specific activity of 3000 mumols/min per mg. 2. Molecular mass of the native enzyme was 45 kDa. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that the native enzyme comprises two identical 27-kDa subunits. 3. Specific enzyme activity increases with increasing concentration of enzyme protein and approaches a plateau at high enzyme concentrations. 4. Enzyme activity increases gradually and nonlinearly with increasing concentration of enzyme in the low concentration range. Above a certain concentration the increase attains a maximal and constant slope. 5. The kinetic properties can be explained by assuming dissociation of the enzyme into subunits with low or no activity.
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