Ligand-binding properties of the glutathione-binding protein of the mussel, Mytilus edulis

Aisling Power, Ronan McCarthy, Elaine Raggett, David Sheehan

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The glutathione-binding protein of Mytilus edulis possesses only one tryptophan per polypeptide. Quenching of intrinsic fluorescence due to this residue was studied in the presence of glutathione S-transferase ligands; hematin, bilirubin, biliverdin, bromosulphophthalein, 1-anilino-8-naphthalene sulphonate, 1,2-dichloro-4-nitrobenzene, ethacrynic acid and sodium deoxycholate as well as in the presence of triethyltin bromide. K(d) values were estimated from these experiments and were found to be 38-310 μM. Based on non-denaturing electrophoresis, the protein was found to have a native molecular weight of 50 kDa. Taken together with previously reported subunit molecular weights in the region of 25 kDa, this indicates that this protein has a dimeric quaternary structure.

Original languageBritish English
Pages (from-to)439-443
Number of pages5
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume115
Issue number4
DOIs
StatePublished - 1996

Keywords

  • binding
  • detoxification
  • fluorescence
  • glutathione
  • mussel
  • Mytilus edulis
  • transferase
  • xenobiotic

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