PMID: 6967312May 1, 1980Paper

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

The Biochemical Journal
A AbbondanzaF Serafini-Cessi

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.

Citations

Feb 1, 1990·Kidney International·J K HortonJ D Williams
Jan 1, 1987·Kidney International·M S ShachnerV T Andriole
Nov 1, 1993·Kidney International·D C RhodesJ A Rhodes
Mar 1, 1984·Bioscience Reports·F Serafini-CessiN Malagolini
Jan 25, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Tsai-Hung WuChang-Youh Tsai
Jan 1, 1986·Virchows Archiv. A, Pathological Anatomy and Histopathology·G Zanetti
Apr 21, 2006·Glycoconjugate Journal·Franca Serafini-CessiDaniela Cavallone
Feb 6, 1999·The Journal of Biological Chemistry·M Tandai-HirumaA Kobata
Oct 23, 2003·The Journal of Biological Chemistry·Daniela CavalloneFranca Serafini-Cessi
Apr 1, 2021·Journal of Cellular and Molecular Medicine·Lufeng BaiMinghui Zhao
Oct 2, 2003·American Journal of Kidney Diseases : the Official Journal of the National Kidney Foundation·Franca Serafini-CessiDaniela Cavallone

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