title: Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci.
abstract: Babesia hylomysci was found to contain two superoxide dismutase (SOD) isoenzymes with isoelectric points (pI) of 4.9 and 5.2. The two isoenzymes (45 and 47 kDa) were composed of two subunits of 22 kDa. An unique amino terminal sequence was determined up to 34 residues from the pooled isoenzymes and was identified as a sequence of SOD. The comparison of this N-terminal sequence of B. hylomysci SOD with 29 known Fe- or Mn-SODs showed more homologies with Fe-SODs.
authors.affiliation: INSERM U42, Villeneuve d'Ascq, France.
authors.forename: P
authors.initials: P
authors.lastname: Becuwe
authors.forename: J
authors.initials: J
authors.lastname: van Beeumen
authors.forename: B
authors.initials: B
authors.lastname: Samyn
authors.forename: J P
authors.initials: JP
authors.lastname: Touzel
authors.forename: C
authors.initials: C
authors.lastname: Slomianny
authors.forename: D
authors.initials: D
authors.lastname: Camus
authors.forename: D
authors.initials: D
authors.lastname: Dive
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001403:Babesia / Q000201:enzymology*; D007527:Isoenzymes / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013482:Superoxide Dismutase / Q000302:isolation & purification*
chemical_list: D007527:Isoenzymes; D013482:Superoxide Dismutase