从人Tamm-Horsfall糖蛋白中分离出的一种糖肽的特性。与白细胞凝集素和抗（人Tamm-Horsfall糖蛋白）抗体的相互作用。
Properties of a glycopeptide isolated from human Tamm-Horsfall glycoprotein. Interaction with leucoagglutinin and anti-(human Tamm-Horsfall glycoprotein) antibodies.
作者信息
Abbondanza A, Franceschi C, Licastro F, Serafini-Cessi F
出版信息
Biochem J. 1980 May 1;187(2):525-8. doi: 10.1042/bj1870525.
Abstract
A sialylated glycopeptide isolated after Pronase digestion of human Tamm-Horsfall glycoprotein behaves as a powerful monovalent hapten in the precipitin reaction between human Tamm-Horsfall glycoprotein and leucoagglutinin, but fails to inhibit the interaction of the glycoprotein with rabbit anti-(human Tamm-Horsfall glycoprotein) antibodies. The glycopeptide is much less active than the intact glycoprotein as an inhibitor of lymphocyte transformation induced by leucoagglutinin.
摘要
在对人Tamm-Horsfall糖蛋白进行链霉蛋白酶消化后分离得到的一种唾液酸化糖肽，在人Tamm-Horsfall糖蛋白与白细胞凝集素之间的沉淀反应中表现为一种强效单价半抗原，但不能抑制该糖蛋白与兔抗（人Tamm-Horsfall糖蛋白）抗体的相互作用。作为白细胞凝集素诱导的淋巴细胞转化抑制剂，该糖肽的活性远低于完整的糖蛋白。
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