Hamazaki H
Department of Biology, Kitasato University School of Medicine, Kanagawa, Japan.
Biochem Biophys Res Commun. 1988 Jan 15;150(1):212-8. doi: 10.1016/0006-291x(88)90507-4.
Human serum amyloid P component (SAP) was found to agglutinate erythrocytes in the presence of calcium ion. The hemagglutination was strongly inhibited by hyaluronic acid as well as by heparan sulfate and dermatan sulfate, but not by chondroitin 4-sulfate and keratan sulfate. A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP.
人们发现,人血清淀粉样蛋白P成分(SAP)在钙离子存在的情况下会使红细胞发生凝集。透明质酸以及硫酸乙酰肝素和硫酸皮肤素可强烈抑制这种血凝反应,但硫酸软骨素4和硫酸角质素则无此作用。透明质酸、硫酸乙酰肝素和硫酸皮肤素可阻断SAP与琼脂糖(SAP的一种特异性配体)的结合,这一事实也证实了SAP与这些糖胺聚糖存在特异性结合。