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A lead-absorbing protein with superoxide dismutase activity from Streptomyces subrutilus

Lookup NU author(s): Dr Ian Hancock

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Abstract

A lead binding protein was purified from the culture filtrate of Streptomyces subrutilus P5. The subunit and native molecular weights were estimated to be 28 and 55 kDa, respectively, indicating that the protein was composed of two identical subunits. The inhibition pattern, the metal content analysis and the EPR spectrum confirmed that the protein was a superoxide dismutase containing Fe and Zn (FeZnSOD). The protein precipitated immediately upon mixing with lead ions and the saturation number of lead ions was about 1100 lead atoms per subunit. Using this property, lead ions could be effectively removed from solutions. © 2001 Federation of European Microbiological Societies.

Publication metadata

Author(s): Hancock IC; So N-W; Rho J-Y; Kim J-H

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 2001

Volume: 194

Issue: 1

Pages: 93-98

ISSN (print): 0378-1097

ISSN (electronic): 1574-6968

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1016/S0378-1097(00)00514-0

DOI: 10.1016/S0378-1097(00)00514-0

PubMed id: 11150672

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