| Literature DB >> 10812074 |
A R Coker1, A Purvis, D Baker, M B Pepys, S P Wood.
Abstract
The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross-beta 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.Entities:
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Year: 2000 PMID： 10812074 DOI： 10.1016/s0014-5793(00)01530-1
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124