Biochemical and immunochemical characterization of Caenorhabditis elegans metallothioneins I and II induced by cadmium.
Metallothioneins in Caenorhabditis elegans (CeMT-I and II) were purified by the combination of gel filtration, ion-exchange chromatography, and high-performance liquid chromatography. Amino acid compositions and amino-terminal sequences of CeMT-I and II were slightly different from those of vertebrate MTs previously reported, although cysteine residue contents were relatively high. Enzyme immunoassay using anti-CeMT-II antibody showed the difference of antigenicity to rat MT-I and II and even to CeMT-I. Immunohistochemical staining revealed the existence of CeMT-II in the intestine and the eggs, suggesting the role of MT in detoxification and homeostasis of heavy metals.
Kondo
M
M
Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Imagawa
M
M
Maruyama
K
K
Okada
Y
Y
Tsunasawa
S
S
Nishihara
T
T
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000917:Antibody Formation; D002104:Cadmium / Q000494:pharmacology*; D002107:Caenorhabditis; D002851:Chromatography, High Pressure Liquid; D007124:Immunoenzyme Techniques; D008668:Metallothionein / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D000596:Amino Acids; D002104:Cadmium; D008668:Metallothionein