Properties of a glycopeptide isolated from human Tamm-Horsfall glycoprotein. Interaction with leucoagglutinin and anti-(human Tamm-Horsfall glycoprotein) antibodies.

نویسندگان

  • A Abbondanza
  • C Franceschi
  • F Licastro
  • F Serafini-Cessi
چکیده

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.

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منابع مشابه

Specific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean).

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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, fo...

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The development of a radioimmunoassay procedure for the estimation of Tamm-Horsfall glycoprotein in human serum.

1. A quantitative radioimmunoassay was developed for the measurement of nanogram amounts of Tamm-Horsfall (TH) glycoprotein in the presence of serum proteins at concentrations above 30 mg/ml. 2. Specific anti-(TH-glycoprotein) antibodies were labelled with 125I and these were usable for a period of 8 weeks. 3. Agarose beads (Sepharose 4B), to which TH-glycoprotein had been coupled via cyanogen ...

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عنوان ژورنال:
  • The Biochemical journal

دوره 187 2  شماره 

صفحات  -

تاریخ انتشار 1980