{"refrec":{"BRefID":32410,"RR":"<b>Das, K.; Jacob, V.; Bouquegneau, J.-M.</b> (2002). White sided dolphin metallothioneins: purification, characterisation and potential role. <i>Comp. Biochem. Physiol. 131(3)</i>: 245-251. <a href=\"https://dx.doi.org/10.1016/S1532-0456(02)00011-X\" target=\"_blank\">https://dx.doi.org/10.1016/S1532-0456(02)00011-X</a>","BEntID":32410,"PublicFlag":1,"CheckedFlag":1,"wosflag":null,"vabbflag":null,"RefStringPartII":". <i>Comp. Biochem. Physiol. 131(3)</i>: 245-251. <a href=\"https://dx.doi.org/10.1016/S1532-0456(02)00011-X\" target=\"_blank\">https://dx.doi.org/10.1016/S1532-0456(02)00011-X</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Das, K.; Jacob, V.; Bouquegneau, J.-M.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Das, K. <i>et al.</i>","Englishabstract":"Metallothioneins (MTs) were characterised in the kidneys of a white-sided dolphin <i>Lagenorhynchus acutus</i> 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. 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