Dowling, V,McDonagh, B,Cotter, EM,O'Brien, N,van Pelt, F,O'Halloran, J,Sheehan, D;

2006

June

Comparative Biochemistry and Physiology Part D :Genomics & Proteomics

Two-dimensional electrophoresis analysis of glutathione affinity-selected proteins from the clam Tapes semidecussatus: Evidence for tissue-specific expression of redox proteins

Validated

()

proteomics Tapes semidecussatus glutathione transferase affinity chromatography ecotoxicology redox status MYTILUS-EDULIS RUDITAPES-DECUSSATUS OXIDATIVE STRESS S-TRANSFERASE BLUE MUSSEL CARBONYLATION PURIFICATION EVOLUTION APOPTOSIS BINDING

1

267

272

Proteins from gill, digestive gland and mantle of the clam Tapes semidecussatus were selected on glutathione (GSH) agarose to simplify proteomic comparison. Analysis by two-dimensional gel electrophoresis (213 SDS PAGE) revealed tissue-specific patterns of protein expression with some spots common to all tissues. Immunoblotting of gill and digestive gland separations identified some spots as glutathione transferases (GSTs). In gill and digestive gland several spots were immunoblotted with Pi class GSTs indicating multiple isoenzymes. Selected spots were excised, digested with trypsin and analyzed by reversed phase C-18 high performance liquid chromatography and tandem mass spectrometry. This confirmed that gill and digestive gland share some GST isoenzymes. Our results suggest that this clam expresses a complex tissue-specific pattern of GSH-binding proteins, which may reflect different redox requirements in each tissue. (c) 2006 Elsevier Inc. All rights reserved.

DOI 10.1016/j.cbd.2006.01.002