- 영문명
- The Purification and Characterization of Macrolide-Phosphotransferase Kof Escherichia coli 209K Highly Resistant to Erythromacin
- 발행기관
- 대한약학회
- 저자명
- 김숙경(Sook Kyung Kim) 오태권(Tae Gwon Oh) 백문창(Moon Chang Baek) 홍종수(Jong Soo Hong) 김병각(Byong Kak Kim) 최응칠(Eung Chil Choi)
- 간행물 정보
- 『약학회지』제41권 제3호 (1997년), 359~364쪽, 전체 6쪽
- 주제분류
- 의약학 > 기타의약학
- 파일형태
- 발행일자
- 1997.06.30
국문 초록
영문 초록
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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