Characterization of Cu,Zn superoxide dismutase from the bathophile fish, Lampanyctus crocodilus.
Cu,Zn SOD from the bathophile teleost Lampanyctus crocodilus (LSOD) shows a high degree of homology with the sequence of the enzymes from other teleostean fish species. The catalytic properties of LSOD are very similar to those of the bovine enzyme, albeit with higher sensitivity to thermal denaturation. The apparent molecular mass of LSOD (37.6 KDa) is higher than the other Cu,Zn SOD variants studied. The aminoacid sequence of LSOD reveals interesting substitutions compared to the bovine enzyme. These are discussed in view of the particular environmental conditions to which L. crocodilus is adapted.
Capo
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Department of Biology, University of Rome Tor Vergata, Italy.
Stroppolo
M E
ME
Galtieri
A
A
Lania
A
A
Costanzo
S
S
Petruzzelli
R
R
Calabrese
L
L
Polticelli
F
F
Desideri
A
A
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D012754:Sharks; D013482:Superoxide Dismutase / Q000737:chemistry* / Q000378:metabolism
D013482:Superoxide Dismutase