Toggle Main Menu Toggle Search

Open Access padlockePrints

The Newcastle University research output collection, currently available on ePrints, will shortly be moving to a new open repository platform, Figshare. To prepare for the data migration we have paused adding new content to ePrints, and will resume once the new repository is launched. During this time you will continue to have access to ePrints (but no new content will appear). We will share updates here when available.

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

Lookup NU author(s): Dr Ian Hancock

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

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

Altmetrics

Altmetrics provided by Altmetric

Share