Application of chemically desialylated and degalactosylated human glycophorin for induction and characterization of anti-Tn monoclonal antibodies.

Human erythrocyte glycophorin was desialylated by mild acid hydrolysis and degalactosylated by Smith degradation. Two monoclonal antibodies (Tn5 and Tn56) obtained by immunization of mice with this 'artificial' Tn antigen were characterized and compared in some experiments with two antibodies (BRIC111 and LM225) obtained in other laboratories by immunization with Tn erythrocytes. The specific binding of the antibodies to glycophorins desialylated and degalactosylated on the nitrocellulose blot and to asialo-agalactoglycophorin-coated ELISA plates, and reactions with authentic Tn antigen served for identification of their anti-Tn specificity.

Analysis of peptidic epitopes recognized by the three monoclonal antibodies specific for the same region of glycophorin A but showing different properties.

Analysis of epitopes for the three monoclonal antibodies (GPA105, GPA33, OSK4-1) against glycophorin A (GPA) was performed with the use of proteolytic fragments of GPA, the synthetic nonapeptide with the sequence of amino acid residues 35-43 of GPA, and a series of peptides synthesized on plastic pins. The antibodies were specific for a short peptide sequence RAHE (a.a.

Monoclonal antibodies against human haptoglobin.

Three monoclonal antibodies: 2.36.71.

The Thomsen-Friedenreich antigen on human urothelial cell lines detectable by peanut lectin and monoclonal antibody raised against human glycophorin A.

The Thomsen-Friedenreich (TF) antigen is a cryptic disaccharide structure on human erythrocytes which can be exposed by neuraminidase treatment and which is supposed to be expressed in an unmasked form on some carcinoma cells. For its detection in addition to auto-, allo- and heteroantisera, PNA (peanut lectin) is being applied. In the present studies the mouse monoclonal antibody (MoAb) raised to asialoglycophorin from human erythrocytes was used.

Specific killing of mouse leukemic cells with ricin A-chain immunotoxin.

Monoclonal IgM antibody against L1210V leukemia was coupled with ricin A-chain using N-succinimidyl 3-(2-pyridyldithio) propionate (SPDP) as a cross--linking agent. The coniugate had potent concentration--dependent cytotoxicity against L1210V, L1210 and RL male 1 cells being completely non toxic to EL-4, P388, RPC-5 and mouse bone marrow cells. The minimum time required for killing L120V leukemia cells was 30h of in vitro exposure, at a concentration 10(-6) M (as assessed by trypan blue test).