Dear ABRF BBS members,
I have a colleague who is interested in measuring the levels of
homocysteine thiolactone in serum. There is evidence that this
thiolactone forms and then modifies proteins by acylating lysine
residues under circumstances where homocysteine is elevated in serum.
There is a thin layer chromatography method in the literature using the
incorporation of [35S]homocysteine into proteins but this is not
applicable to the samples that my colleague wishes to analyze. Does
anyone know other ways to detect this amino acid? Can you suggest an
alternate way to measure the thiolactone (or proteins that have been
modified by it) that could be applied to clinical samples?
Thanks in advance for your input.
ml
-- Mark O. Lively, Ph.D. Professor of Biochemistry Wake Forest University School of Medicine Medical Center Blvd. Winston-Salem, North Carolina 27157 Voice: 336-716-2969 Fax: 336-716-7200 email: mlively@wfubmc.edu
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