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  • Title: Purification and characterization of 5'-phosphodiesterase from barley rootlets.
    Author: Wang AY, Juang RH, Chang CT, Sung HY.
    Journal: Biochem Mol Biol Int; 1993 Apr; 29(6):1095-102. PubMed ID: 7687182.
    Abstract:
    A phosphodiesterase was purified from barley rootlets by polyethylene glycol fractionation, calcium phosphate gel-cellulose adsorption, Sepharose CL-4B gel filtration, DEAE-Sepharose CL-6B ion exchange and preparative polyacrylamide gel electrophoresis (PAGE). The enzyme was purified by 103.6 folds and 11% of the enzyme activity was recovered. The purified enzyme was apparently homogeneous when examined on PAGE. It had a molecular weight of 100 kD, an optimum pH of 9.5, and a Km of 0.28 mM on the hydrolysis of p-nitrophenyl thymidine 5'-phosphate. SDS-PAGE revealed that the enzyme molecule might be composed of two or three subunits. Reducing agents, CuSO4, EDTA and 5'-nucleotides were inhibitory to the enzyme activity. This enzyme was able to hydrolyze RNA and denatured DNA efficiently, whereas native DNA was not a good substrate.
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