The primary structure of iron superoxide dismutase from Escherichia coli
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 r...
Saved in:
Published in | FEBS letters Vol. 221; no. 1; pp. 87 - 90 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
31.08.1987
Elsevier |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | 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. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(87)80357-5 |