- 期刊
Purification and Biochemical Properties of β-Lactamase from Escherichia Coli Ntuh 9501-1
並列摘要
Penicillin β-lactamase (penicillinase) was purified from a strain of Escherichia coli NTUH 9501-1 resistant to ampicillin and other β-lactam antibiotics. The purified enzyme preparation gave a single band on sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and its molecular weight was around 26,000 from SDS-PAGE. Its isoelectric point was 6.2 and the optimal pH was about 6.4. The ehnzyme activity was inhibited by 1 mM of Hg++, Ca++, Mg++, Fe++ and sulbactam, whereas the enzyme was not inhibited by the same concentration of EDTA, GDTA, Cu++ and Zn++. The enzymological properties of the purified preparation have been compared with those of β-lactamase from other gram-negative bacteria and the biochemical data indicate that the purified β-lactamase is plasmid-mediated penicillinase.
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