title: Low-molecular weight metalloproteins in tissues of the narwhal (Monodon monoceros).
abstract: Narwhal (Monodon monoceros) liver and kidney cytosol were fractionated by gel chromatography, anion-exchange chromatography and electrophoresis. Cadmium was associated largely with low molecular weight proteins, while mercury was associated also with high molecular weight proteins, but apparently not because of saturation of the metallothionein mechanism. Eight different electrophoretic bands, four of which were metalloproteins, were found under the "metallothionein" peak. Anion-exchange chromatography yielded five metal peaks while further fractionation on G-50 gave two peaks, one containing almost pure metallothionein (Mt-1) and the other a metalloprotein having twice the molecular weight of metallothionein. Mt-2 was observed, at a much lower concentration than Mt-1, in liver but not kidney.
mesh_terms: D000818:Animals; D002104:Cadmium / Q000032:analysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000032:analysis; D004589:Electrophoresis, Disc; D005399:Fishes / Q000378:metabolism*; D007668:Kidney / Q000032:analysis; D008099:Liver / Q000032:analysis*; D008628:Mercury / Q000032:analysis; D008667:Metalloproteins / Q000032:analysis*; D008668:Metallothionein / Q000032:analysis; D008970:Molecular Weight; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D013056:Spectrophotometry, Ultraviolet
chemical_list: D008667:Metalloproteins; D002104:Cadmium; D008668:Metallothionein; D008628:Mercury