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J. Biol. Chem., Vol. 258, Issue 1, 91-96, Jan, 1983
BL Beaman, SM Scates, SE Moring, R Deem and HP Misra
A unique form of superoxide dismutase was isolated and characterized from
Nocardia asteroides GUH-2. This enzyme contains 1 to 2 g atoms each of Fe,
Mn, and Zn per mol and exhibits spectral properties suggestive of Fe- or
Mn-containing superoxide dismutases. Its Mr = 100,000, and it is composed
of four subunits of equal size which are not covalently joined. The amino
acid composition of the enzyme was more closely related to the Mn- or
Fe-containing enzymes of Mycobacterium species and was least related to the
Cu-Zn enzyme of eukaryotes. Azide at 1 and 20 mM inhibits the activity 10
and 41%, respectively, and 5 mM H2O2 inhibits 40%, but 1 or 5 mM cyanide
caused trivial effect. The immunofluorescent staining, which was specific
for superoxide dismutase of N. asteroides, indicated the association of
this enzyme to the outer cell wall of the organism. Further, the enzyme was
shown to be selectively secreted into the medium.
Purification and properties of a unique superoxide dismutase from Nocardia asteroides
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