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Changes in the histidine residues of Cu/Zn superoxide dismutase during aging
Author(s) -
Santa Maria Consuelo,
Revilla Elisa,
Ayala Antonio,
de la Cruz Cristina P.,
Machado Alberto
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01083-q
Subject(s) - histidine , superoxide dismutase , chemistry , biochemistry , enzyme
Cu/Zn‐Superoxide dismutase activity (Cu/Zn‐SOD) was studied in liver from 3‐ and 24‐month‐old rat. A significant decrease of enzyme activity in liver of the aged rat was found. Various amino acid residues and protein carbonyl groups (CO) were measured in purified young and old enzyme. It was found that the ‘old’ enzyme had one histidine fewer and higher CO content than the ‘young’ Cu/Zn‐SOD. Inactivation ‘in vitro’ of purified commercial bovine erythrocyte Cu/Zn‐SOD led to a decrease in the enzymatic activity, an increase in the CO and one histidine residue modified. A similar behavior between aging and oxidation was suggested.