Soelter J, Uhlenbruck G
Immunology. 1986 May;58(1):139-44.
Human C-reactive protein (CRP) shows binding specificities for phosphate monoesters, polycations and for several other biological macromolecules lacking these ligands. We report here that the formerly observed interaction of CRP with snail galactans, as exemplified by Helix pomatia galactan, is not due to a lectin-like carbohydrate-binding reactivity, but, instead that CRP obviously binds to phosphate groups that are minor constituents of these polysaccharides. Structural analysis of the galactan revealed that the phosphate groups are attached by a, as yet unidentified, linkage group to the carbohydrate backbone. Thus, the anti-galactan reactivity of CRP can be attributed to the protein's classical anti-phosphate/anti-phosphorylcholine specificity.
人C反应蛋白（CRP）对磷酸单酯、聚阳离子以及其他几种缺乏这些配体的生物大分子具有结合特异性。我们在此报告，先前观察到的CRP与蜗牛半乳聚糖（如苹果螺半乳聚糖为例）的相互作用，并非由于类似凝集素的碳水化合物结合反应性，而是相反，CRP明显结合到这些多糖的次要成分磷酸基团上。对半乳聚糖的结构分析表明，磷酸基团通过一个尚未确定的连接基团连接到碳水化合物主链上。因此，CRP的抗半乳聚糖反应性可归因于该蛋白经典的抗磷酸/抗磷酸胆碱特异性。
