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Proteomic characterization of novel serum amyloid P component variants from human plasma and urine
Author(s) -
Kiernan Urban A.,
Nedelkov Dobrin,
Tubbs Kemmons A.,
Niederkofler Eric E.,
Nelson Randball W.
Publication year - 2004
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200300690
Subject(s) - serum amyloid p component , chemistry , urine , proteome , valine , amyloid (mycology) , sialic acid , mass spectrometry , glycan , proteomics , biochemistry , blood proteins , chromatography , amino acid , glycoprotein , biology , gene , immunology , inorganic chemistry , c reactive protein , inflammation
Serum amyloid P component (SAP) is a human plasma protein that has been widely studied for its influence on amyloid plaque formation and stabilization. SAP was characterized directly from human plasma and urine samples via novel affinity mass spectrometry‐based proteomic technology that is able to readily discriminate between mass‐altered protein variants. These analyses were able to identify several variants of SAP that have not been previously reported. These variants include microheterogeneity of the glycan structure, from the loss of one or both terminal sialic acid residues, as well as the loss of the C ‐terminal valine residue. Moreover, the analysis of urine allowed for the consistent identification of serum amyloid P component as a normal constituent of the urine proteome.