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Characterization of a Human Cervical Carcinoma-associated Antigen by Lectin Binding and Immuno-electron Microscopy by J. J. Wang; S. R. Roffler; M. H. Yu; C. S. Yin; M. Y. Yeh is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The specific binding and nature of the epitope recognized by monoclonal antibody (Mab) 1H10, which binds an antigen expressed on human cervical tumors, was characterized by enzyme digestion, lectin competition assay and immuno-electron microscopy. Membrane homogenates of CaSki cervical carcinoma cells were digested with various enzymes, then analysed by SDS-PAGE and immunoblotting. Cells grown on coverslips were treated with various enzymes and in situ binding of Mab 1H10 to cells was analysed by electron microscopy. The ability of lectin-conjugates to block Mab 1H10 binding to CaSki cells was also examined. Treatment of samples with sodium periodate abrogated antigen recognition by Mab 1H10. Neuraminidase and hyaluronidase digestion decreased but did not eliminate Mab 1H10 binding to cells in situ. Chondroitinase ABC digestion, in contrast, removed Mab 1H10 binding sites both in vitro and in situ. Trypsin and chymotrypsin digestion of cell membrane homogenates decreased the molecular weight of the Mab 1H10 antigen but did not decrease the binding intensity. Wheat germ agglutinin (WGA) strongly bound to CaSki cells and partially blocked Mab 1H10 binding, indicating that the antigen

Who reads Characterization of a Human Cervical Carcinoma-associated Antigen by Lectin Binding and Immuno-electron Microscopy?

Author

J. J. Wang; S. R. Roffler; M. H. Yu; C. S. Yin; M. Y. Yeh

Publisher

Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC (ISSN 1432-119X)

Published

1992

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)