未成熟人类胸腺细胞上花生凝集素结合糖蛋白的鉴定
Identification of peanut agglutinin-binding glycoproteins on immature human thymocytes.
作者信息
De Maio A, Lis H, Gershoni J M, Sharon N
出版信息
Cell Immunol. 1986 May;99(2):345-53. doi: 10.1016/0008-8749(86)90243-1.
Previous studies in our laboratory have shown that peanut agglutinin (PNA), a lectin specific for the disaccharide Gal beta 3GalNAc, binds to immature (cortical) thymocytes of mouse and man and not to the mature (medullary) cells. Using lectin overlay of protein blots and lectin-affinity chromatography, we have found that the major PNA-binding glycoproteins on total as well as on immature (PNA+) human thymocytes correspond to two bands of Mr 170,000 and 180,000. Another glycoprotein, of Mr 110,000, also binds PNA but to a lesser extent. All three glycoproteins contain sialic acid as demonstrated by cell surface labeling with NaIO4-NaB3H4, binding of wheat germ agglutinin, and reaction with alkaline phosphatase-hydrazide. After treatment with sialidase, binding of PNA to these glycoproteins is significantly enhanced.
我们实验室之前的研究表明，花生凝集素（PNA）是一种对二糖Galβ3GalNAc具有特异性的凝集素，它能与小鼠和人类的未成熟（皮质）胸腺细胞结合，而不与成熟（髓质）细胞结合。通过蛋白质印迹的凝集素覆盖法和凝集素亲和层析法，我们发现，总人胸腺细胞以及未成熟（PNA+）人胸腺细胞上主要的PNA结合糖蛋白对应于两条分子量分别为170,000和180,000的条带。另一种分子量为110,000的糖蛋白也能结合PNA，但结合程度较低。通过用NaIO4-NaB3H4进行细胞表面标记、小麦胚凝集素的结合以及与碱性磷酸酶酰肼的反应证明，所有这三种糖蛋白都含有唾液酸。用唾液酸酶处理后，PNA与这些糖蛋白的结合显著增强。
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