| Literature DB >> 7535252 |
M Sugiyama1, T Kumagai, H Matsuo, M Z Bhuiyan, K Ueda, H Mochizuki, N Nakamura, J E Davies.
Abstract
The bleomycin-binding proteins designated BLMA and BLMS, which confer resistance to bleomycin (Bm), from Bm-producing Streptomyces verticillus ATCC15003 and a methicillin-resistant Staphylococcus aureus B-26, respectively, were overexpressed in Escherichia coli. The present study showed that both BLMA and BLMS quench the antibacterial activity of Bm by the binding to the drug. To immuno-characterize the Bm-binding proteins, we constructed a monoclonal antibody against BLMA. The antibody, designated 893-12, did not cross react to BLMS and another Bm-binding protein from tallysomycin-producing Streptoalloteichus hindustanus. Although the ability of Bm to cleavage DNA was eliminated by a binding of BLMA to Bm, as shown by Sugiyama et al. [Gene 151 (1994) 11-15], the Bm-induced DNA degradation was restored by pre-incubation of BLMA with the anti-BLMA monoclonal antibody.Entities:
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Year: 1995 PMID: 7535252 DOI: 10.1016/0014-5793(95)00218-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124