Zinc deficient bovine erythrocyte superoxide dismutase has low specific activity.
Zinc deficient bovine superoxide dismutase (Cu2E2SOD (E = empty)) was prepared and purified by high performance liquid chromatography (HPLC). Each peak was characterized as to protein, copper content and specific activity. The Cu2E2SOD peak fractionated by HPLC has a low specific activity at pH 7.8 (about 10% of the native enzyme (Cu2Zn2SOD)). With the addition of zinc ions, the specific activity of Cu2E2SOD was quantitatively restored to that of the native enzyme. This behavior implies that the zinc ion is very important for the appearance of enzyme activity.
Hirose
J
J
Department of Food Science and Technology, Faculty of Engineering, Fukuyama University, Hiroshima, Japan.
Kano
H
H
Kidani
Y
Y
Iwamoto
H
H
Hiromi
K
K
D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004912:Erythrocytes / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet; D013482:Superoxide Dismutase / Q000097:blood* / Q000302:isolation & purification; D015032:Zinc / Q000378:metabolism*
D013482:Superoxide Dismutase; D015032:Zinc