NDLI: Metallomics investigations on potential binding partners of methylmercury in tuna fish muscle tissue using complementary mass spectrometric techniques

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Metallomics investigations on potential binding partners of methylmercury in tuna fish muscle tissue using complementary mass spectrometric techniques

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Metallomics investigations on potential binding partners of methylmercury in tuna fish muscle tissue using complementary mass spectrometric techniques

Content Provider	Royal Society of Chemistry (RSC)
Author	Sanz-Medel, Alfredo Kutscher, Daniel J. Bettmer, Jörg
Copyright Year	2012
Abstract	In this study, the binding behaviour of methylmercury (MeHg+) towards proteins is investigated. Free sulfhydryl groups in cysteine residues are known to be the most likely binding partners, due to the high affinity of mercury to sulphur. However, detailed knowledge about discrete binding sites in living organisms has been so far scarce. A metallomics approach using different methods like size-exclusion chromatography (SEC) and liquid chromatography (LC) coupled to inductively coupled plasma-mass spectrometry (ICP-MS) as well as complementary mass spectrometric techniques (electrospray ionisation-tandem mass spectrometry, ESI-MS/MS) are combined to sequence and identify possible target proteins or peptides after enzymatic digestion. Potential targets for MeHg+ in tuna fish muscle tissue are investigated using the certified reference material CRM464 as a model tissue. Different extraction procedures appropriate for the extraction of proteins are evaluated for their efficiency using isotope dilution analysis for the determination of total Hg in the extracts. Due to the high chemical stability of the mercury–sulphur bond, the bioconjugate can be quantitatively extracted with a combination of tris(hydroxymethyl)aminomethane (TRIS) and sodium dodecyl sulphate (SDS). Using different separation techniques such as SEC and SDS-polyacrylamide gel electrophoresis (SDS-PAGE) it can be shown that major binding occurs to a high-molecular weight protein (Mw > 200 kDa). A potential target protein, skeletal muscle myosin heavy chain, could be identified after tryptic digestion and capillary LC-ESI-MS/MS.
Starting Page	807
Ending Page	813
Page Count	7
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	4
Issue Number	8
Journal	Metallomics
DOI	10.1039/c2mt20055d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Polyacrylamide gel electrophoresis Thiol Cysteine Isotope Lauric acid Gel electrophoresis Electrospray ionization Certified reference materials High-performance liquid chromatography Protein Skeletal muscle SEC Tuna Sodium Methylmercury Myosin Covalent bond Size-exclusion chromatography Bioconjugation Molar mass distribution U.S. Securities and Exchange Commission Mass spectrometry Nucleophile
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Metallomics investigations on potential binding partners of methylmercury in tuna fish muscle tissue using complementary mass spectrometric techniques