-transparent.png){kind=logo}
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.
Related Publications
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
November 1984,
Bioscience reports,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
January 2004,
Organic & biomolecular chemistry,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
April 2002,
Microbiology (Reading, England),
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
November 1979,
The Biochemical journal,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
March 1984,
Bioscience reports,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
April 1996,
FEBS letters,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
October 1977,
International journal of peptide and protein research,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
October 1980,
Pathology,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
March 2015,
Asian Pacific journal of allergy and immunology,
A Abbondanza, and
C Franceschi, and
F Licastro, and
F Serafini-Cessi
March 1983,
Clinica chimica acta; international journal of clinical chemistry,
