The complete amino acid sequence of iron superoxide from Escherichia coli has been determined. The sequence was deduced from analysis of peptides obtained after cleavage of the carboxymethylated apoenzyme with trypsin. Stapholococcus aureus protease or CNBr. The polypeptide chain is made up of 192 residues and is easily aligned with the other known amino acid sequences of iron and manganese superoxide dismutases from various sources. The iron superoxide dismutase from E. coli shows a significantly higher homology with the iron enzyme from a different organism than with the manganese isoenzyme from E. coli.
The primary structure of iron superoxide dismutase from Escherichia coli / Schinina', Maria Eugenia; Maffey, L; Barra, Donatella; Bossa, Francesco; Puget, K; Michelson, Am. - In: FEBS LETTERS. - ISSN 0014-5793. - 221:(1987), pp. 87-90. [10.1016/0014-5793(87)80357-5]
The primary structure of iron superoxide dismutase from Escherichia coli
SCHININA', Maria Eugenia;BARRA, Donatella;BOSSA, Francesco;
1987
Abstract
The complete amino acid sequence of iron superoxide from Escherichia coli has been determined. The sequence was deduced from analysis of peptides obtained after cleavage of the carboxymethylated apoenzyme with trypsin. Stapholococcus aureus protease or CNBr. The polypeptide chain is made up of 192 residues and is easily aligned with the other known amino acid sequences of iron and manganese superoxide dismutases from various sources. The iron superoxide dismutase from E. coli shows a significantly higher homology with the iron enzyme from a different organism than with the manganese isoenzyme from E. coli.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
