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Purification and characterization of manganese superoxide dismutase from Ganoderma microsporum
Author(s) -
Pan ShuMei,
Ye JrShin,
Hseu RueyShyang
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203491
Subject(s) - isoelectric point , superoxide dismutase , size exclusion chromatography , chemistry , biochemistry , ion chromatography , amino acid , ganoderma , microsporum canis , enzyme , ammonium sulfate precipitation , chromatography , biology , microbiology and biotechnology , ganoderma lucidum , food science , antifungal
Manganese superoxide dismutase (Mn‐SOD) in the mycelium of Ganoderma microsporum was purified to homogeneity by heat treatment at 70°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 isoeleetric focusing. Comparisons of 17 amino acids from the N‐terminus ofMn‐SOD subunit with the derived amino acid sequences from the reported Mn‐SOD eDNA 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.