I have a known protein and subject it to glycation via methylglyoxal. After the reaction has been completed I would like to know whether Arg (Lys) residues have been modified by methlyglyoxal. Does anyone know a company or institute that provides the analysis of protein modifications (e. g., via LC/MS-MS)? Thanks for your help.
Dear Christian
I'm sorry to guide you. I have no ideas of the companies involved in what you ask. I hope the relevant RG researchers in this field provide you with useful information
Regards
you know the protein, you know that you have glycated it . digest it with trypsin and check the fragments in MALDI-Tof. trypsin digests at Arg-Lys bond, if you see a bigger peptide at that specific Arg, then your issue is solved. this will work only if your glycation reaction is highly specific to that particular Arg residue. you can even check it on a HPLC the glycated one may elute at diffterent time/% of polarity.
You can always send your protein for MS analysis to Children's Hospital of Philadelphia protein and proteomics core facility.
Dear Christian,
if you wish you can send your protein for MS analysis to BioPharmaSpec. Check the website out.
http://biopharmaspec.com
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