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KMID : 0370219970410030359
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Yakhak Hoeji
1997 Volume.41 No. 3 p.359 ~ p.364
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The Purification and Characterization of Macrolide-Phosphotransferase Kof Escherichia coli 209K Highly Resistant to Erythromacin
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김숙경/Kim SK
오태권/백문창/홍종수/김병각/최응칠/Oh TG/Baek MC/Hong JS/Kim BK/Choi EC
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Abstract
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Resistance gene mphK was cloned from Escherichia coli 209K strain which is highly resistant to erythromycin (EM). By using the cloned plasmid pGE64, E. coli NM522 was transformed. The comparison of macrolide-phosphotransferase K [MPH(K)] activity between E. coli 209K and E. coli NM522(pGE64) showed that the total enzyme activity of MN522(pGE64) was fifty-fole higher than that of 209K. To identify characteristics of MPH(K) more precisely. MPH(K) was isolated and purified from the NM522 (pGE64). The final purification f MPH(K) through several stages of purification process was 89 fole and the overall recovery was 11%. This enzyme was monomer with the molecular weight of 34 kDa and its isoelectric point (pI) was 5.0. The optimal pH and temperature for activity were 8.0 and 40oC, respectively.
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