Wu A M, Watkins W M, Song S C, Herp A, Wu J H
Glyco-immunochemistry Research Laboratory, Chang-Gung Medical College, Tao-Yuan, Taiwan, Republic of China.
Biochem Biophys Res Commun. 1995 Apr 6;209(1):103-10. doi: 10.1006/bbrc.1995.1476.
The binding properties of human Tamm-Horsfall Sd(a+) urinary glycoprotein(THGP) and asialo-THGP with various applied lectins was investigated by quantitative precipitin and precipitin inhibition assays. Both glycoproteins completely precipitated Abrus precatorius agglutinin(APA). They also reacted well with Wistaria floribunda (WFA), Glycine max (soybean, SBA), and Ricinus communis agglutinins and precipitated over 78% of the lectin nitrogen added, but reacted poorly or weakly with all alpha-anomeric GalNAc specific lectins, such as Helix pomatia (HPA), Phaseolus lunatus (lima bean, LBL), and Maclura pomifera (MPL) lectins. The glycoprotein-lectin interaction was inhibited by GalNAc beta 1-->, Gal beta 1-->4GlcNAc, or by both. The findings suggest that Sd (a+) THGP and asialo-THGP are among the best water-soluble glycoprotein ligands for GalNAc beta 1-->and Gal beta 1-->4GlcNAc active lectins.
通过定量沉淀和沉淀抑制试验,研究了人Tamm-Horsfall Sd(a+)尿糖蛋白(THGP)和去唾液酸THGP与各种应用凝集素的结合特性。两种糖蛋白都能使相思子凝集素(APA)完全沉淀。它们也能与紫藤凝集素(WFA)、大豆凝集素(SBA)和蓖麻凝集素良好反应,并沉淀超过78%添加的凝集素氮,但与所有α-异头型GalNAc特异性凝集素,如苹果蜗牛凝集素(HPA)、利马豆凝集素(LBL)和桑橙凝集素(MPL)反应较差或较弱。糖蛋白-凝集素相互作用受到GalNAcβ1-->、Galβ1-->4GlcNAc或两者的抑制。研究结果表明,Sd(a+)THGP和去唾液酸THGP是GalNAcβ1-->和Galβ1-->4GlcNAc活性凝集素的最佳水溶性糖蛋白配体之一。