Title Pruification and Characterization of Superoxide Dismutse from Rhodotorula glutinis K-24
Author Jung, Sang Yun · Lee, Sang Ok · Lee, Tae Ho *
Address Department of Microgiology, College of Natural Science, Pusan National University
Bibliography Korean Journal of Microbiology, 31(6),573-578, 1993
DOI
Key Words superoxide dismutase, SOD of Rh. glutinis, Fe-SOD of eukaryotes
Abstract Superoxide dismutase (SOD) was pruified from Rhodotorula glutinis K-24 to an electrophoretically homogeneous state and partially characterized. SOD was purified by aceticacid treatment, ammonium sulfate fractionation, column chromatographies on DEAE-Sephadex A-50, Sephadex G-100, phenyl-Toyopearl 650 M, and hydroxyapatite. The molecular weight and subunit molecular weight of the purified enzyme were estimated to be 40.000 and 19,000, respectively. The isoelectric point of the enzyme was about pH 4.9. The purified enzyme remained stable at pH 8.0-11.0, 25℃ for 40 hrs, but was rapidly inactivated below 8.0. SOD was stable up to 60℃ at pH 8.0 with about 80% relative activity but was rapidly inactivated at higher temperatures. The enzyme was insensitive to cyanide and fluoride, and sensitive to hydrogen peroxide and azide. The results suggested that the enzyme was an iron-containing SOD.
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