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Superoxide dismutase in strains of the genusFlavobacterium:isolation and characterization

โœ Scribed by M. Sanchez-Moreno; M. Monteoliva-Sanchez; F. Ortega; A. Ramos-Cormenzana; M. Monteoliva


Publisher
Springer
Year
1989
Tongue
English
Weight
355 KB
Volume
152
Category
Article
ISSN
0302-8933

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โœฆ Synopsis


Two electrophoretically different forms of superoxide dismutase, one of them containing manganese-protein and the other iron-protein, were detected in eleven different strains of the genus Flavobacterium. The activities of the different strains were similar to those described for other bacteria. The two molecular forms of the enzyme differed clearly with regard to activity, electrophoretic behaviour, sensitivity to cyanide and peroxide, and NaC1 requirement. Both molecular forms were isolated from Flavobacterium halmephilum. Molecular mass absorption spectra, metal content, optimum pH, heat-sensitivity and stability were described.


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Thylakoid-bound superoxide dismutase (SOD; EC 1.15.1.1) was solubilized by Triton X-100 from spinach and purified to a homogeneous state. The molecular weight of thylakoid-bound SOD was 52000; the enzyme was composed of two equal subunits. Its activity was not sensitive to cyanide and hydrogen perox