COMPLETE AMINO-ACID-SEQUENCES OF 5 DIMERIC AND 4 MONOMERIC FORMS OF METALLOTHIONEIN FROM THE EDIBLE MUSSEL MYTILUS-EDULIS

EA MacKay, Julian Overnell, B Dunbar, I R Davidson, P E Hunziker, J H R Kagi, J E Fothergill

Research output: Contribution to journalArticlepeer-review

Abstract

Cadmium-induced metallothioneins from the common sea mussel, Mytilus edulis, were shown to comprise of two groups of isoforms having apparent molecular masses of 10 kDa and 20 kDa. The 10-kDa group was resolved by anion-exchange chromatography into four fractions while the 20-kDa group was resolved into three fractions using this method. After metal removal and S-methylation of the cysteine residues using methyl-p-nitrobenzenesulphonate the complete amino acid sequences were determined. Five isoforms of the 20-kDa group were shown to possess monomeric units consisting of 71 amino acids. These proteins were distinct from the four 72-amino-acid proteins of the 10-kDa group. The FASTA algorithm has been used to compare the degree of similarity between the mussel metallothionein MT-10-IV isoform and other metallothioneins. The mussel MT-10-IV isoform exhibited substantial similarity to other molluscan metallothioneins. Moreover, the mussel metallothionein exhibited more similarity to vertebrate metallothioneins than to those of non-molluscan invertebrates, thus suggesting that the mussel metallothioneins are class I metallothioneins.
Original languageEnglish
Pages (from-to)183-194
Number of pages12
JournalEUR J BIOCHEM
Volume218
Issue number1
Publication statusPublished - 1993

Keywords

  • Biochemistry & Molecular Biology
  • GROWTH INHIBITORY FACTOR
  • RAINBOW-TROUT
  • CDNA SEQUENCES
  • MOLLUSCAN METALLOTHIONEINS
  • CAENORHABDITIS-ELEGANS
  • MOLECULAR-CLONING
  • RAT-LIVER METALLOTHIONEIN-2
  • CADMIUM-BINDING-PROTEINS
  • COPPER
  • ALZHEIMERS-DISEASE

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