1980
DOI: 10.1016/s0300-9084(80)80288-4
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Préparation et forme sérique de la protéine réactive C de lapin

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Cited by 14 publications
(6 citation statements)
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“…Pontet et al (38) have suggested that CRP in acute-phase rabbit serum exists entirely in a high molecular weight form due to complexing with LDL, but like Kushner and Somerville (26), we have been unable to reproduce this observation using either gel fltration or density gradient ultracentrifugation (M. L. Baltz and M. B. Pepys, unpublished observations).…”
Section: Discussionmentioning
confidence: 61%
“…Pontet et al (38) have suggested that CRP in acute-phase rabbit serum exists entirely in a high molecular weight form due to complexing with LDL, but like Kushner and Somerville (26), we have been unable to reproduce this observation using either gel fltration or density gradient ultracentrifugation (M. L. Baltz and M. B. Pepys, unpublished observations).…”
Section: Discussionmentioning
confidence: 61%
“…Interaction of pentraxins with lipoproteins has been suggested in previous studies, although the results have appeared inconsistent. Interaction between CRP and LDL or VLDL that contain apolipoprotein B or apoE have been reported (Pontet et al, 1979;Cabana et al, 1982). The greatest correlation appeared for apolipoprotein B (Rowe et al, 1984a).…”
Section: Discussionmentioning
confidence: 98%
“…While early studies suggested that human CRP was associated with lipids or lipoproteins (McLeod & Avery, 1941; Wood, 1963;Saito & Hara, 1968), more recent results suggest that interaction is limited to aggregated CRP (DeBeer et al, 1982b;Rowe et al, 1984a;Saxena et al, 1987) or abnormal lipoproteins (Rowe et al, 1984a,b). Rabbit CRP usually shows a complex with low-density lipoproteins (Pontet et al, 1979;Cabana et al, 1982), and affinity adsorption showed CRP-dependent removal of lipoproteins containing apolipoproteins E (apoE) and B (Rowe et al, 1984a). Interaction of rabbit pentraxins with lipoproteins may be of low affinity and is not detected by sucrose density gradient ultracentrifugation [reviewed in Pepys et al (1985)].…”
mentioning
confidence: 99%
“…Another possibility is that an acute-phase apolipoprotein could be responsible for the binding. Three LPSinduced, lipoprotein-associated, acute-phase proteins are serum amyloid A (17,35), C-reactive protein (7,27), and arylesterase (5). Serum amyloid A is present in affinitypurified complexes of LPS-LP formed in acute-phase sera (35), but it is not known whether it leads to formation of the complexes or whether it is present on lipoprotein particles that bind to LPS through a different mechanism.…”
Section: Methodsmentioning
confidence: 99%