Microbiol. Biotechnol. Lett. 2000; 28(5): 251-257
Serratia marcescens Purine Nucleoside Phosphorylase의 정제 및 특성
Purification and Properties of Serratia marcescens Purine Nucleoside Phosphorylase.
Serratia marcescens purine nucleoside phosphorylase (PNP) was purfied to homogeneity by streptomycin sulfate treatment, Sephacry HR S-200 gel filtration chromatography and AMP-agarose affinity chromatography. The specific activity of the enzyme was increased 49-fold during purification with an overall yield of 7.0%. The molecular weight was 168kD as estimated by Sephadex G-150 gel filtration chromatography. The S. marcescens enzyme was composed of six identical subunits with subunit molecular weight of 28kD, as estimated by SDS-PAGE. The Km values of S. marcescens enzyme for inosine and deoxyinsoine were 0.38 and 1.20 mM, respectively. The ph optimum was near 8.0, and the enzyme was relatively heat-stable protein. The enzyme was inactivated com-pletely by 0.5 mM of
Keywords: purine nucleoside phosphorylase, purification, purification, properties, Seratia marcescens
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