| Literature DB >> 3129309 |
M Barthélémy1, J Péduzzi, H Ben Yaghlane, R Labia.
Abstract
SHV-2 beta-lactamase was purified from an overproducing variant of a clinical isolate of Escherichia coli resistant to cefotaxime. Pure protein was digested by trypsin and Lys-C endoproteinase. Proteolytic peptides, isolated by reverse-phase HPLC, were submitted to manual Edman degradation and aligned by homology with the sequence of SHV-1 beta-lactamase. A putative amino acid sequence was deduced. Structural comparison revealed that SHV-2 differed from SHV-1 by only one amino acid, Gly----Ser, at position 213 of the mature protein.Entities:
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Year: 1988 PMID: 3129309 DOI: 10.1016/0014-5793(88)80734-8
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124