Abstract
This report shows a new approach for linking the boronated polylysine(BPL) at specific sites on the antibody that are distant from the antigen binding site, that is, to the group made functional by oxidation of the carbohydrate residues present at the CH2 region of the antibody. By this technique we estimate that over 104 boron atoms are bound per antibody molecule without demonstrable loss of immunoreactivity.
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References
Alam F., Soloway A.H., Barth R.F., Mafune N., Adams D.M. & Knoth W.H. (1989) J. Med. Chem. 32, 2326–2330.
Barth R.F., Adams D.M., Soloway A.H., Mechetner E.B., Alam F. & Anisuzzaman ABK (1991) Anal. Chem. 63, 890–892.
Pettersson M.L., Courel M.N., Girard N., Abraham R., Gabel D., Thellier M. & Delpech B. (1990) J. Immunol. Meth. 126, 95–102.
Rodwell J.D., Alvarez V.L., Lee C., Lopes A.D., Goers J.W.F, King H.D., Posner H.J. & McKearn T.J (1986) Proc. Nat. Acad. Sc. (US) 82, 2632–2636.
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© 1993 Springer Science+Business Media New York
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Novick, S. et al. (1993). Binding of Boronated Polylysine to Immunoglobulin by Way of Glycoside Moieties: Immunoreactivity and Boron Content. In: Soloway, A.H., Barth, R.F., Carpenter, D.E. (eds) Advances in Neutron Capture Therapy. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2978-1_74
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DOI: https://doi.org/10.1007/978-1-4615-2978-1_74
Publisher Name: Springer, Boston, MA
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Online ISBN: 978-1-4615-2978-1
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