1 Ocak 2015 Dergi makalesi Açık Erişim

Eksin, Ece; Erdem, Arzum

Citation Style Language JSON

{
  "DOI": "10.1039/c4ra13303j", 
  "abstract": "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.", 
  "author": [
    {
      "family": "Eksin", 
      "given": " Ece"
    }, 
    {
      "family": "Erdem", 
      "given": " Arzum"
    }
  ], 
  "container_title": "RSC ADVANCES", 
  "id": "77337", 
  "issue": "7", 
  "issued": {
    "date-parts": [
      [
        2015, 
        1, 
        1
      ]
    ]
  }, 
  "page": "4774-4779", 
  "title": "Electrochemical detection of N-homocysteinylated BSA in the fetal bovine serum medium", 
  "type": "article-journal", 
  "volume": "5"
}