Qiping Ruan

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A uridine phosphorylase(UPase) was isolation from Enterobacter aerogenes EAM-Z1 and purified by means of ammonium sulfate precipitation, DEAE-cellulose, Phenyl-Sepharose, DEAE-Sepharose, FPLC ion exchange, and Sephacryl S-200 column chromatography. The purified UPase showed homogeneity on the native polacrylamide gel electrophoresis. The UPase is a trimer(More)
It has been previously shown that Escherichia coli L-asparaginase II (L-ASP) signal peptide is capable of being utilized to direct extracellular secretion of hirudin III (HV3) in shake flask. In this study HV3 muteins R33G34D35(S36)-HV3 were generated by introduction of adhesive recognition sequence RGD(S) into the non-functional region of HV3. The(More)
Conditions for biotransformation and purification of FUR were investigated. The result showed that when the cell concentration of E. aerogenes was 10% (w/v), the temperature and pH were 7.8 and 60 degrees C respectively, 59.7% UR was converted to FUR. It also demonstrated that the ideal procedure for the purification of FUR is silica gel column(More)
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