Molecular chaperone properties of serum amyloid P component

Alun R. Coker, Alan Purvis, Douglas Baker, Mark B. Pepys, Steve P. Wood

Research output: Contribution to journalArticlepeer-review


The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross-β fold suggests a possible chaperone role. Here we show that human SAP enhances the refolding yield of denatured lactate dehydrogenase and protects against enzyme inactivation during agitation of dilute solutions. These effects are independent of calcium ions and are not inhibited by compounds that block the amyloid recognition site on the B face of SAP, implicating the A face and/or the edges of the SAP pentamer. We discuss the possibility that the chaperone property of SAP, or its failure, may contribute to the pathogenesis of amyloidosis.
Original languageEnglish
Pages (from-to)199-202
Number of pages4
JournalFEBS Letters
Issue number2
Early online date9 May 2000
Publication statusPublished - 12 May 2000


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