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

被引：6
作者：
Dowling, V.
McDonagh, B.
Cotter, E. M.
O'Brien, N.
van Pelt, F.
O'Halloran, J.
Sheehan, D.
机构：
[1] Natl Univ Ireland Univ Coll Cork, Dept Biochem, Proteom Res Grp, Cork, Ireland
[2] Natl Univ Ireland Univ Coll Cork, Environm Res Inst, Cork, Ireland
[3] Natl Univ Ireland Univ Coll Cork, Dept Food Sci, Cork, Ireland
[4] Natl Univ Ireland Univ Coll Cork, Dept Pharmacol & Therapeut, Cork, Ireland
[5] Natl Univ Ireland Univ Coll Cork, Dept Zool Ecol & Plant Sci, Cork, Ireland
来源：
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY D-GENOMICS & PROTEOMICS | 2006年 / 1卷 / 03期
关键词：
proteomics; Tapes semidecussatus; glutathione transferase; affinity chromatography; ecotoxicology; redox status;
D O I：
10.1016/j.cbd.2006.01.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：267 / 272
页数：6
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