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2971652 
Technical Report 
Isolation and partial characterization of a cadmium-binding protein from Lumbriculus variegatus (Oligochaeta, Annelida) 
Bauer-Hilty, A; Dallinger, R; Berger, B 
1989 
BIOSIS/90/14311 
94 
2 
373-380 
English 
BIOSIS COPYRIGHT: BIOL ABS. 1. A low molecular weight, cadmium-binding protein has been isolated from Lumbriculus variegatus. 2. The protein has an apparent molecular weight of 19 kD as estimated by Sephadex G-75 chromatography and is thought to be a dimer. It shows high absorbance at 254 nm and low absorbance at 280 nm. 3. Amino acid analysis revealed a high content of cysteine (16.5%), and elevated amounts of aspartate (10.9%), serine (10.6%), glutamate (9.3%), glycine (11.7%), leucine (10%) and lysine (10%). The content of aromatic amino acids was low. 4. After SDS-polyacrylamide gel electrophoresis three distinct bands with molecular weights of 19, 11.5 and 10.2 kDa, respectively, were found. The three bands are assumed to represent the dimer, the monomer and a partially carboxymethylated monomer. 5. The protein is suggested to play an important role in the detoxification of cadmium.