CHROMATOGRAPHIC ANALYSIS OF METALLOTHIONEIN PROTEINS FROM THE CRAB SPECIES SCYLLA-SERRATA AND PORTUNUS-PELAGICUS

Different chromatographic techniques have been used successfully to isolate and purify two copper-binding proteins and a zinc-binding ligand from the hepatopancreas of the crab Portunus pelagicus. Comparison studies were made using the crab Scylla serrata which had been studied previously. Based on the identical purification protocol and the very similar retention times on reversed phase HPLC, the copper-binding proteins are found to be similar to those from the crab Scylla serrata and are shown to be metallothioneins. Reversed phase HPLC analysis confirms that there are two distinct forms as purified by standard molecular sieve and ion exchange chromatography.