Human recombinant CuZn-superoxide dismutase. Amino acid sequence and location of the disulfide bond.
The complete amino acid sequence of recombinant human Cu-Zn superoxide dismutase (CuZnSOD) is presented. The S-carboxymethylated protein was cleaved at lysine residues (with Achromobacter protease I) to provide a set of nine non-overlapping fragments accounting for 90% of the sequence. These fragments were then overlapped and aligned, and the sequence was completed by using peptides generated by cleavage at glutamic acid residues (with S. aureus V8 protease) and at arginine (with clostripain). The recombinant protein contains a single disulfide bond between cysteine residues 57 and 146. The primary sequence of recombinant human CuZnSOD is identical to that predicted by its cDNA sequence.
Peretz
M
M
Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
Werber
M U
MU
Burstein
Y
Y
D000421:Alcaligenes / Q000201:enzymology; D000595:Amino Acid Sequence; D001120:Arginine; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000378:metabolism; D004229:Dithiothreitol; D010450:Endopeptidases; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry*; D012697:Serine Endopeptidases; D013482:Superoxide Dismutase / Q000737:chemistry*
D004220:Disulfides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D001120:Arginine; D013482:Superoxide Dismutase; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D004229:Dithiothreitol