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The primary structure of human erythrocyte copper zinc super oxide dis mutase cleavage with staphylococcus aureus protease determination of the amino terminal blocking group and location of the di sulfide bond

, : The primary structure of human erythrocyte copper zinc super oxide dis mutase cleavage with staphylococcus aureus protease determination of the amino terminal blocking group and location of the di sulfide bond. Italian Journal of Biochemistry (English Edition) 31(1): 39-48

Results obtained after digestion of copper/zinc superoxide dismutase from human erythrocytes with S. aureus protease are described. Peptides soluble in alkaline conditions were essential for completing the determination of the primary structure of the enzyme; other peptides were important for establishing the amidation state of dicarboxylic amino acid residues and for confirming controversial sequences. The human enzyme was acetylated at the NH2 terminus and contained an intrasubunit disulfide bond connecting half-cystine residues 57 and 146.

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