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Purification and Characterization of Purine Nucleoside Phosphorylase (PNP) in Micrococcus luteus

The journal of microbiology v.34 no.1 , 1996년, pp.82 - 89  

Purine nucleoside phosphorylase (PNP) was purified in Micrococcus luteus (M. luteus) using streptomycin sulfate and amomonium sulfate fractionation, three times by a Sephadex G-100 gel filtration and a DEAE-Sephadex A-50 ion exchange chromatography. The enzyme was purified 72 folds with a 11% recovery and showed a single band in a nondenaturing gel electrophoresis. The M. W. of PNP turned out to be 1.35 * 10$^{5}$ delton in G-150 gel filtration chromatography. The stability of the enzyme was increased by treatment with both substrates, MgCI$_{2}$ or CaCI$_{2}$, but not significantly kcal/mol. M. luteus PNP catalyzed the phosphorolysis of inosine, deoxyinosine, guanosine and deoxyguanosine with the Km value of 1.5 * 10$^{-3}$ M, 3.0 * 10$^{-3}$ M, 5.0 * 10$^{-4}$ M, respectively. The enzyme was reacted with adenosine, 1-methylnosine and 1-methylguanosine as substrates, which were shown to be poor substrates for mammalian enzyme.

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이 논문을 인용한 문헌 (3)

  1. 1996. "" The journal of microbiology, 34(3): 270~273 
  2. 1997. "" The journal of microbiology, 35(1): 15~20 
  3. 2000. "Purification and Properties of Serratia marcescens Purine Nucleoside Phosphorylase." 산업미생물학회지 = Korean journal of applied microbiology and biotechnology, 28(5): 251~257 


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