Purification and characterization of manganese superoxide dismutase from Ganoderma microsporum.
Manganese superoxide dismutase (Mn-SOD) in the mycelium of Ganoderma microsporum was purified to homogeneity by heat treatment at 70 degrees C, ammonium sulfate fractionation, DEAE-52 anion-exchange chromatography, and Sephacryl SH-200 chromatography. The molecular mass of its native form was estimated to be 98 kD by size-exclusion chromatography. This enzyme is tetrameric composed of four subunits of equal size of 25 kD. The pI of this purified Mn-SOD was located at pH 6.34 and 5.06 by isoelectric focusing. Comparisons of 17 amino acids from the N-terminus of Mn-SOD subunit with the derived amino acid sequences from the reported Mn-SOD cDNA clones of other sources indicated a high degree of homology among the Ganoderma genus but the Mn-SOD from G. microsporum showed a high variation when compared with other organisms.
Pan
S M
SM
Department of Botany, National Taiwan University, Taipei, Republic of China. pan@ccms.edu.ntu.tw
Ye
J S
JS
Hseu
R S
RS
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005658:Fungi / Q000201:enzymology*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013482:Superoxide Dismutase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism
D013482:Superoxide Dismutase