|White sided dolphin metallothioneins: purification, characterisation and potential role|Das, K.; Jacob, V.; Bouquegneau, J.-M. (2002). White sided dolphin metallothioneins: purification, characterisation and potential role. Comp. Biochem. Physiol. 131(3): 245-251. dx.doi.org/10.1016/S1532-0456(02)00011-X
In: Comparative Biochemistry and Physiology. Pergamon Press: London; New York. ISSN 0010-406X, more
marine mammals; Lagenorhynchus acutus; white-sided dolphin; heavymetals; cadmium; metallothioneins; isoforms
|Authors|| || Top |
- Das, K., more
- Jacob, V.
- Bouquegneau, J.-M., more
Metallothioneins (MTs) were characterised in the kidneys of a white-sided dolphin Lagenorhynchus acutus stranded along the Belgian coast, displaying high levels of cadmium (Cd) and mercury (Hg) in liver and kidney. The protein has two isoforms: MT-1 and MT-2. MT-1 binds Cu, Zn, Hg and Cd, while MT-2 only binds Zn, Hg and Cd. This suggests different metabolic functions for the two isoforms: MT-1 is mainly involved in Cu homeostasis; MT-2, which was fourfold more abundant than MT-1, detoxifies most of the accumulated cadmium.