Chromatographic analysis of low-molecular-mass copper-binding ligands from the crab species Scylla serrata and Portunus pelagicus.
Two copper-binding proteins and a zinc-binding ligand were isolated from the hepatopancreas of the crab Portunus pelagicus. The copper-binding proteins behave similarly to those from the crabs Carcinus maenas and Scylla serrata, and were shown to be metallothioneins. Reversed-phase high-performance liquid chromatographic (HPLC) analysis confirmed the relative purity of both proteins with only cross-contamination between the two different forms of metallothioneins, and offers a good method to separate the two forms of metallothioneins. The vast difference in the retention times (and hence the hydrophobicity) in reversed-phase HPLC indicates that the two proteins could be conformationally very different.
Ang
S G
SG
Department of Chemistry, National University of Singapore.
Wong
V W
VW
D000818:Animals; D003386:Brachyura / Q000737:chemistry*; D003300:Copper / Q000378:metabolism*; D008024:Ligands; D008099:Liver / Q000737:chemistry; D008297:Male; D008668:Metallothionein / Q000378:metabolism; D008970:Molecular Weight; D010179:Pancreas / Q000737:chemistry; D013045:Species Specificity; D013056:Spectrophotometry, Ultraviolet
D008024:Ligands; D003300:Copper; D008668:Metallothionein