LaMont J T, Isselbacher K J
J Cell Physiol. 1977 Mar;90(3):565-72. doi: 10.1002/jcp.1040900318.
Neuraminidase-treated human erythrocytes, but not untreated erythrocytes, were agglutinated by concanavalin A. The degree of concanavalin A agglutinability was not directly related to sialic acid removal by neuraminidase. While maximal sialic acid release was obtained with 5 units neuraminidase/2 x10(9) erythrocytes, maximal concanavalin A agglutination was only obtained after exposure to 20 units neuramindase. Binding of 3H-concanavalin A by erythrocytes was 10-fold higher with rabbit compared to human red cells. Neuraminidase treatment of human erythrocytes caused a relative increase in 3H-concanavalin binding, but the absolute amount was still 10-fold less than that bound to rabbit erythrocytes. Specific adherence of neuraminidase to Con A-Agarose could not be demonstrated. There was no evidence for contamination of the neuraminidase preparation with proteases using a sensitive assay. These studies suggest that neuraminidase absorbs to erythrocytes by a mechanism other than removal of sialic acid.
经神经氨酸酶处理的人红细胞会被伴刀豆球蛋白A凝集，而未经处理的红细胞则不会。伴刀豆球蛋白A的凝集程度与神经氨酸酶去除唾液酸的程度并无直接关联。当每2×10⁹个红细胞使用5单位神经氨酸酶时可实现最大程度的唾液酸释放，但只有在暴露于20单位神经氨酸酶后才会出现最大程度的伴刀豆球蛋白A凝集。与人类红细胞相比，兔红细胞对³H-伴刀豆球蛋白A的结合能力高10倍。对人红细胞进行神经氨酸酶处理会使³H-伴刀豆球蛋白的结合相对增加，但绝对量仍比与兔红细胞结合的量少10倍。未证实神经氨酸酶与伴刀豆球蛋白A-琼脂糖存在特异性结合。使用灵敏的检测方法未发现神经氨酸酶制剂被蛋白酶污染的证据。这些研究表明，神经氨酸酶通过去除唾液酸以外的机制吸附到红细胞上。
