Examining serum amyloid P component microheterogeneity using capillary isoelectric focusing and MALDI-MS

Noah G. Weiss, Jason W. Jarvis, Randall W. Nelson, Mark Hayes

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Serum amyloid P component (SAP) is a glycoprotein of interest due to its presence in amyloid plaque formations. As with most glycoproteins, SAP can possibly vary greatly in its isoforms, which can be an important factor toward understanding the role of SAP. Interestingly, previous characterizations suggest varying degrees of microheterogeneity, some of which are in conflict. In this work, we provide new information to clarify SAP's microheterogeneity profile using CIEF to carefully analyze pooled samples and by studying individual samples across populations with mass spectrometric immunoassay. With respect to CIEF, a single pI band was observed suggesting that human SAP does not have extensive heterogeneity concluded from gel IEF experiments in the past. Additionally, this is supported by a population study, which revealed an overwhelming degree of uniformity. Overall, this work corroborates the idea that SAP is relatively consistent across the population and with respect to microheterogeneity.

Original languageEnglish (US)
Pages (from-to)106-113
Number of pages8
JournalProteomics
Volume11
Issue number1
DOIs
StatePublished - Jan 1 2011

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Keywords

  • Glycoproteomics
  • IEF
  • Isoforms
  • MS
  • Serum amyloid P

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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