[Purification and some properties of superoxide dismutase from Fusarium moniliform].
Superoxide dismutase from Fusarium moniliform was purified by the steps including heating, ammonium sulfate fractionation, Sephedax G-100 gel filtration and DEAE-Sephadex A-50 chromatography. The results showed that the enzyme was a Mn-SOD with the specific activity of 2640 U/mg and had two homogenous subunits whose molecular mass were 14.5 kD. The wave length of max. absorbing peak in ultraviolet spectrum was 276 nm which was not similar with other resource of SOD. The composition of amino acid was also analyzed.
Kou
R
R
Institute of Molecular Science, Shanxi University, Taiyuan.
Bai
Y
Y
Yuan
J
J
Chu
X
X
D000596:Amino Acids / Q000032:analysis; D005670:Fusarium / Q000201:enzymology*; D008970:Molecular Weight; D013482:Superoxide Dismutase / Q000737:chemistry / Q000302:isolation & purification*
D000596:Amino Acids; D013482:Superoxide Dismutase