Publication | Open Access
Bovine Erythrocyte Superoxide Dismutase
219
Citations
48
References
1974
Year
Animal PhysiologyProtein ChemistryBiochemistryProtein FoldingMedicineIdentical SubunitsNatural SciencesMolecular BiologyDerived PeptidesProtein Mass SpectrometryReactive Oxygen SpecieProteomicsRedox BiologyIntact Polypeptide ChainOxidative Stress
Abstract The complete primary structure of reduced and S-carboxy-methylated bovine erythrocyte superoxide dismutase has been derived through analysis of peptides from peptic, plasmin, and hydroxylamine digests of the intact polypeptide chain, and from chymotryptic, subtilisin, and dilute acid digests of derived peptides. From these data, the following unique amino acid sequence of 151 residues was deduced, corresponding to a molecular weight of 15,600, in each of the 2 apparently identical subunits of the protein molecule. (Cmc denotes S-carboxymethylcysteine.) [see PDF for equation]
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