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pubmed-article:18571492pubmed:abstractTextHomocysteine (Hcy) is incorporated into protein via a reaction of the thioester Hcy-thiolactone with epsilon-amino group of a protein lysine residue. This reaction leads to impairment and alteration of protein's function and has been implicated in atherothrombotic disease. However, the data regarding N-linked Hcy content in proteins are limited, mostly due to a lack of facile assays. Here I describe a new sensitive assay for the determination of protein N-linked Hcy and demonstrate its utility for individual proteins and biological fluids. N-linked Hcy is liberated from proteins by acid hydrolysis and converted to Hcy-thiolactone, which is then purified and quantified by high-performance liquid chromatography on a cation exchange column. The quantification is by fluorescence after postcolumn derivatization with o-phthaldialdehyde. Using this assay, the levels of N-linked Hcy in individual pure proteins were found to vary from as high as 0.470-0.515 mol/mol protein for human and equine ferritins to as low as 0.00006 mol/mol protein for chicken lysozyme. Hemoglobins from a variety of species contained more N-linked Hcy than did corresponding albumins (0.0127-0.0828 vs. 0.0027-0.0086 mol/mol). Normal human plasma and milk were found to contain submicromolar concentrations of protein N-linked Hcy, whereas cow milk and whey contained micromolar concentrations of protein N-linked Hcy.lld:pubmed
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pubmed-article:18571492pubmed:year2008lld:pubmed
pubmed-article:18571492pubmed:articleTitleNew method for the determination of protein N-linked homocysteine.lld:pubmed
pubmed-article:18571492pubmed:affiliationDepartment of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, International Center for Public Health, Newark, NJ 07101, USA. jakubows@umdnj.edulld:pubmed
pubmed-article:18571492pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18571492pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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