Dishon T, Finkel R, Marcus Z, Ginsburg I
Immunology. 1967 Dec;13(6):555-64.
Various streptococcal species produce an haemosensitizing factor during the logarithmic phase of growth. A variety of mammalian cells sensitized with this factor become agglutinated following the addition of antistreptoccocal serum and also undergo cytopathic changes in the presence of complement. The haemosensitizing factor is thermostable and is unaltered by trypsin, papain, chymotrypsin, lipases or ribonucleases. Attempts to destroy the binding sites on the cell membrane by treatment with phospholipase C from or by neuraminidase failed. Treatment with trypsin or papain on the other hand markedly increased the binding capacity of red blood cell for the haemosensitizing factor. Studies on the nature of the binding sites on the erythrocyte membrane of the haemosensitizing factor suggest that cholesterol and phospholipids constitute some of the binding sites for this factor.
多种链球菌在生长对数期产生一种溶血致敏因子。用该因子致敏的多种哺乳动物细胞在加入抗链球菌血清后会发生凝集,并且在补体存在的情况下会发生细胞病变。溶血致敏因子具有热稳定性,不受胰蛋白酶、木瓜蛋白酶、胰凝乳蛋白酶、脂肪酶或核糖核酸酶的影响。用来自产气荚膜梭菌的磷脂酶C或神经氨酸酶处理以破坏细胞膜上的结合位点的尝试均告失败。另一方面,用胰蛋白酶或木瓜蛋白酶处理可显著增加红细胞对溶血致敏因子的结合能力。对溶血致敏因子在红细胞膜上结合位点性质的研究表明,胆固醇和磷脂构成了该因子的一些结合位点。