A lead-absorbing protein with superoxide dismutase activity from Streptomyces subrutilus.
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.
So
N W
NW
Department of Microbiology, College of Natural Sciences, Dan-kook University, Cheon-an 330-714, South Korea.
Rho
J Y
JY
Lee
S Y
SY
Hancock
I C
IC
Kim
J H
JH
D000596:Amino Acids / Q000032:analysis; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007854:Lead / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology* / Q000254:growth & development; D013482:Superoxide Dismutase / Q000737:chemistry / Q000378:metabolism*
D000596:Amino Acids; D002352:Carrier Proteins; C055217:lead-binding proteins; D007854:Lead; D013482:Superoxide Dismutase