Studies of Copper-Binding Behavior of Copper-Free and Apo-superoxide Dismutase by High-Performance Liquid Chromatography

Various enzyme species differing in copper content were formed when various amounts of Cu2+ were added to copper-free superoxide dismutase (E2Zn2SOD) and the apo-enzyme (E2E2SOD), and were separated by high-performance liquid chromatography. The three peaks, I, II and III, arising from the former we...

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Veröffentlicht in:	Chemical & pharmaceutical bulletin 1988/06/25, Vol.36(6), pp.2103-2108
Hauptverfasser:	HIROSE, JUNZO, TOIDA, SHINOBU, KUNO, HARUMI, OZAKI, SATORU, KIDANI, YOSHINORI
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry apo-superoxide dismutase aposuperoxide dismutase Biological and medical sciences Chromatography, High Pressure Liquid copper Copper - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Oxidoreductases Protein Binding superoxide dismutase Superoxide Dismutase - metabolism
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Beschreibung
Zusammenfassung:	Various enzyme species differing in copper content were formed when various amounts of Cu2+ were added to copper-free superoxide dismutase (E2Zn2SOD) and the apo-enzyme (E2E2SOD), and were separated by high-performance liquid chromatography. The three peaks, I, II and III, arising from the former were assigned as Cu2Zn2SOD, CuEZn2SOD and E2Zn2SOD, respectively, based on the copper content and specific activity. The three peaks, A, B and C, from the latter were assigned as Cu2Cu2SOD+Cu2CuESOD, CuEE2SOD+Cu2E2SOD, and E2E2SOD, respectively.
ISSN:	0009-2363 1347-5223
DOI:	10.1248/cpb.36.2103