High-mannose oligosaccharides from human Tamm-Horsfall glycoprotein.
نویسندگان
چکیده
The present communication reports the occurrence of high-mannose oligosaccharides on Tamm-Horsfall glycoprotein prepared from human pooled urine. The Pronase digest of the glycoprotein was fractionated by gel filtration and a high-mannose glycopeptide species was separated from complex-type glycopeptides. When high-mannose glycopeptides were digested with endo-beta-N-acetylglucosaminidase H, followed by reduction with [3H]KBH4, three oligosaccharides were resolved by thin-layer chromatography. On the basis of chromatographic mobility and exoglycosidase digestions the composition Man7-, Man6-, and Man5-GlcNAc was assigned to the three oligosaccharides. Man6GlcNAc is by far the major component.
منابع مشابه
Evaluation of Glycan Profiles of Tamm-horsfall Glycoprotein and Uromodulin
Uromodulin is well-known to be the more potent immunosuppressive glycoprotein isolated from pregnant women urine, compared to its counterpart, Tamm-Horsfall glycoprotein (THP) isolated from non-pregnant women/male urine. However, structural profiles of these glycoproteins were controversial until today. Hence, this paper aims to identify the pregnancy associated glycosylation changes of THP and...
متن کاملProperties of a glycopeptide isolated from human Tamm-Horsfall glycoprotein. Interaction with leucoagglutinin and anti-(human Tamm-Horsfall glycoprotein) antibodies.
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...
متن کاملSpecific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean).
Human Tamm-Horsfall glycoprotein inhibits lymphocyte transformation induced by leucoagglutinin and haemagglutinin from Phaseolus vulgaris (red kidney bean). The glycoprotein interacts with the two lectins, giving insoluble precipitates. The interaction with leucoagglutinin is highly specific, and the shape of the precipitin curve is that of an antigen-antibody reaction; precipitation is specifi...
متن کاملThe presence in serum of proteins which are immunologically cross-reactive with Tamm-Horsfall glycoprotein.
Affinity chromatography, with rabbit anti-(human Tamm-Horsfall glycoprotein) IgG, was applied to the isolation from normal human serum of protein, which is immunologically cross-reactive with the urinary glycoprotein. The antigen-antibody complex was dissociated with the use of sodium thiocyanate solution, a medium which fails to dissociate urinary Tamm-Horsfall glycoprotein-antigen complex. Th...
متن کاملRole of Tamm-Horsfall protein in the binding and in vivo phagocytosis of type 1 fimbriated Escherichia coli by mouse peritoneal macrophages.
Tamm-Horsfall glycoprotein (THP) contains manno-oligosaccharides that are recognized by type 1 fimbriae (F1) of Escherichia coli. In the present study, we examined the in vivo phagocytic activity of mouse peritoneal macrophages after treatment of bacteria with THP. At low THP concentrations (12.5 microg/ml and 50 microg/ml) no significant difference was observed in the phagocytosis of E. coli F...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Bioscience reports
دوره 4 3 شماره
صفحات -
تاریخ انتشار 1984