M. Pontet , M. D'Asnieres , D. Gache , J. Escaig , R. Engler
{"title":"A new pentraxin (serum amyloid P-component) in the rat: Evidence for two quaternary structures and effect of ligands on self-association","authors":"M. Pontet , M. D'Asnieres , D. Gache , J. Escaig , R. Engler","doi":"10.1016/0005-2795(81)90135-5","DOIUrl":null,"url":null,"abstract":"<div><p>A new rat serum protein has been isolated by affinity chromatography using ethanolamine- or phosphoethanolamine-substituted agarose gels. This protein has the morphological and functional characteristics of serum amyloid P-component and C-reactive protein. It comprises C<sub>5</sub> cyclic symmetry structure with non covalently cross-linked subunits which have calcium-dependent binding sites. We have called this protein rat serum amyloid P-component since it has all the properties typical of human serum amyloid P-component: it is made up of 10 subunits, it contains sialic acid and hexoses, it forms macroscopic polymers and it does not precipitate with pneumococcal C-polysaccharide. Rat amyloid P-component has three remarkable properties. Electron microscopy has shown that apart from pentagonal figures and stacked discs, rat P-component has a C<sub>10</sub> cyclic symmetry structure. Rat amyloid P-component has an affinity for specific ligands, such as phosphorylcholine or phosphoethanolamine. These ligands are able to depolymerize self-associated rat P-component. With these characteristics, rat serum amyloid P-component could prove to be an important model in the study of the relations between amyloid P-component and amyloidosis.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90135-5","citationCount":"18","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581901355","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 18
Abstract
A new rat serum protein has been isolated by affinity chromatography using ethanolamine- or phosphoethanolamine-substituted agarose gels. This protein has the morphological and functional characteristics of serum amyloid P-component and C-reactive protein. It comprises C5 cyclic symmetry structure with non covalently cross-linked subunits which have calcium-dependent binding sites. We have called this protein rat serum amyloid P-component since it has all the properties typical of human serum amyloid P-component: it is made up of 10 subunits, it contains sialic acid and hexoses, it forms macroscopic polymers and it does not precipitate with pneumococcal C-polysaccharide. Rat amyloid P-component has three remarkable properties. Electron microscopy has shown that apart from pentagonal figures and stacked discs, rat P-component has a C10 cyclic symmetry structure. Rat amyloid P-component has an affinity for specific ligands, such as phosphorylcholine or phosphoethanolamine. These ligands are able to depolymerize self-associated rat P-component. With these characteristics, rat serum amyloid P-component could prove to be an important model in the study of the relations between amyloid P-component and amyloidosis.