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|Title:||Chromatographic analysis of low-molecular-mass copper-binding ligands from the crab species Syclla serrata and Portunis pelagicus||Authors:||Ang, S.-G.
Thi Wong, V.W.
|Issue Date:||22-May-1992||Citation:||Ang, S.-G.,Thi Wong, V.W. (1992-05-22). Chromatographic analysis of low-molecular-mass copper-binding ligands from the crab species Syclla serrata and Portunis pelagicus. Journal of Chromatography A 599 (1-2) : 21-24. ScholarBank@NUS Repository.||Abstract:||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. © 1992.||Source Title:||Journal of Chromatography A||URI:||http://scholarbank.nus.edu.sg/handle/10635/93310||ISSN:||00219673|
|Appears in Collections:||Staff Publications|
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