Literature DB >> 7589519

Changes in the histidine residues of Cu/Zn superoxide dismutase during aging.

C S Maria1, E Revilla, A Ayala, C P de la Cruz, A Machado.   

Abstract

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.

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Year:  1995        PMID: 7589519     DOI: 10.1016/0014-5793(95)01083-q

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  5 in total

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Journal:  J Biol Chem       Date:  2011-04-25       Impact factor: 5.157

2.  Glycation-induced inactivation and loss of antigenicity of catalase and superoxide dismutase.

Authors:  H Yan; J J Harding
Journal:  Biochem J       Date:  1997-12-01       Impact factor: 3.857

3.  Cloning and expression analysis of Drosophila extracellular Cu Zn superoxide dismutase.

Authors:  Michael J Blackney; Rebecca Cox; David Shepherd; Joel D Parker
Journal:  Biosci Rep       Date:  2014-12-23       Impact factor: 3.840

4.  Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein.

Authors:  Jung Hoon Kang
Journal:  BMB Rep       Date:  2013-11       Impact factor: 4.778

5.  LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess H2O2.

Authors:  Meena Kathiresan; Ann M English
Journal:  Chem Sci       Date:  2016-09-07       Impact factor: 9.825

  5 in total

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