Title Saccharomyces cerevisiae에서 PNP의 부분 정제와 특성
Author 최혜선
Address 울산대학교 미생물학과
Bibliography Korean Journal of Microbiology, 29(3),172-178, 1991
Key Words Purine nucleoside phosphorylase, Saccharomyces cerevisiae, phosphorolysis
Abstract Intracellular purine nucleoside phosphorylase (PNP) from Saccharomyces cerevisiae was partially purified using ammonium sulfate fractionation, heat treatment, a DEAE-Sephadex A-50 anion exchange chromatography and a Sephadex G-100 gel filtration chromatography. The enzyme was purified 20 fold with 3% recovery. The stability of enzyme was kept by addition of inosine and dithiothreitol. The pH optimum was found to be from 6.3 to 7.3 PNP was sensitive to 10mM of Hg^2+, Cu^2+, and was inactivated completely by 2 mM of p-chloromercuribenzoate and 5,5'-dithiobis (2-nitrobenzoate). The enzyme was capable of catalyzing the phosphorolysis of inosine, deoxyinosine, guanosine, deoxyguanosine and adenosine.
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