1 Ocak 2015 Dergi makalesi Açık Erişim

Eksin, Ece; Erdem, Arzum

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        "affiliation": "Ege Univ, Fac Pharm, Dept Analyt Chem, TR-35100 Izmir, Turkey", 
        "name": "Eksin, Ece"
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      {
        "affiliation": "Ege Univ, Fac Pharm, Dept Analyt Chem, TR-35100 Izmir, Turkey", 
        "name": "Erdem, Arzum"
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    "description": "Homocysteine-thiolactone (HTL) is known as an intramolecular thioester of homocysteine (Hcy). The thioester chemistry of Hcy-thiolactone underlies its ability to form isopeptide bonds with the protein lysine residues, which may impair, or alter the function of protein. HTL modification is a unique post-translational protein modification that is recognized as an emergent biomarker for cardiovascular and neurovascular disease. Electrochemical detection of bovine serum albumin (BSA) before and after N-homocysteinylation was performed using a disposable graphite electrode in combination with a differential pulse voltammetry (DPV) technique. Accordingly, an enhanced detection of BSA was obtained based on the changes at the oxidation signal of BSA after N-homocysteinylation. A lower detection limit was obtained for N-homocysteinylated BSA (N-Hcy-BSA) as 1.09 mu g mL(-1) in comparison to the one of non-homocysteinylated BSA (i.e., 1.55 mu g mL(-1)). The DL of BSA and N-Hcy-BSA in fetal bovine serum medium was also calculated and found to be 3.29 mu g mL(-1) and 2.72 mu g mL(-1), respectively.", 
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      "issue": "7", 
      "pages": "4774-4779", 
      "title": "RSC ADVANCES", 
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    "title": "Electrochemical detection of N-homocysteinylated BSA in the fetal bovine serum medium"
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