Amino acid sequence of the small cadmium-binding protein (MP II) from Nereis diversicolor (annelida, polychaeta). Evidence for a myohemerythrin structure.
The primary sequence of the low-molecular-mass cadmium-binding protein metalloprotein II of Nereis diversicolor (Hediste diversicolor, recent denomination) has been determined. This protein is composed of 119 amino acids and has 80.8% identity with the N. diversicolor myohemerythrin [Takagi, T. & Cox, J. A. (1991) FEBS Lett. 285, 25-27]. The fact that iron, which normally binds to myohemerythrin, is not found to be associated with the cadmium-binding protein metalloprotein II in cadmium-exposed animals could be the result of the complete abolition of the iron-binding capacity of the protein due to the binding of cadmium.
Demuynck
S
S
ERS 20 CNRS (Phylogénie moléculaire des Annélides), Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
Li
K W
KW
Van der Schors
R
R
Dhainaut-Courtois
N
N
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D006422:Hemerythrin / Q000031:analogs & derivatives* / Q000737:chemistry; D007525:Isoelectric Focusing; D008668:Metallothionein / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping; D011077:Polychaeta / Q000737:chemistry*; D017421:Sequence Analysis
D006422:Hemerythrin; D010446:Peptide Fragments; C004203:cadmium-binding protein; C008571:myohemerythrin; D008668:Metallothionein