Title Purification and Characterustics of Cytidin Deaminase from Bacillus subtilis ED 213
Author Park, Jung Moon · Kim, Tae Hyun · Yu, Tae Shick *
Address Department of Microbiology, College of Natural Science, Keimyung University
Bibliography Korean Journal of Microbiology, 32(6),545-551, 1994
Key Words cytidine deaminase, Bacillus subtilis ED213
Abstract The cytidine deaminase was putified by about 87 fold with a 10% yield from cell-free extract of Bacillus subtilis ED 213. The purified cytidin deaminase was confirmed to be pure, and showed a single band and a single peak on the poluacrylamide gel electrophoresis and HPLC, respectively. The molecular weight of the enzyme was determined to be about 56,000 by gel filtraion and consisted of four identical subunits having molecular weight of about 14,600 by SDS-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was pH 4.27 and the absorption spectrum of the enzyme has a maximum at 274 nm and a minimum around 250nm. The enzyme was relatively stable between pH 6.0 and pH 8.0, however, it was unstable at 50℃ for 10 minutes resulting in 50% of the normal activity. The cytidin deaminase catalyzed the deaminase of deoxycytidine, 5-methylcytidin, 5-fluorodeoxycytidine, 5-bromocytidine besides cytidine.
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