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Quantification of Thiol-containing amino acids linked by disulfides to LDL

Zinellu, Angelo and Sotgia, Salvatore and Deiana, Luca and Carru, Ciriaco (2005) Quantification of Thiol-containing amino acids linked by disulfides to LDL. Clinical Chemistry, Vol. 51 , p. 658-660. eISSN 1530-8561. Article.

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DOI: 10.1373/clinchem.2004.043943


Several studies have indicated that plasma proteins interact with homocysteine (Hcy) to form stable disulfide-linked products. Hcy in plasma is mainly bound to albumin, but interactions with ceruloplasmin, fibrin, annexin II, and transthyretin have been also reported. In 1991, Olszewski and McCully described the presence of Hcy in lipoproteins in patients with hypercholesterolemia. Because the analysis was performed after acidic hydrolysis of apoprotein, the Hcy measured by these authors was the sum of (a) Hcy incorporated in the primary structure of apolipoprotein B-100 , (b) Hcy thiolactone bound to lysine residues of protein by amide or peptide linkages and converted to Hcy by acidic conditions after release, and (c) Hcy linked to apolipoprotein B-100 (apoB-100) by a disulfide bond.

Item Type:Article
ID Code:685
Uncontrolled Keywords:Homocysteine (Hcy), apolipoprotein B-100, low-density lipoproteins (LDL)
Subjects:Area 05 - Scienze biologiche > BIO/12 Biochimica clinica e biologia molecolare clinica
Divisions:001 Università di Sassari > 01 Dipartimenti > Scienze biomediche
Publisher:American Association for Clinical Chemistry
Deposited On:18 Aug 2009 10:02

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