Abstract
A method has been developed to achieve rapid and reproducible complexation of indium to transferrin at pH 7.4. The system consists of nitrilotriacetic acid (NTA) as the intermediate carrier ligand, whose function is to allow the /sup 113/m In ion, in a solution in Tris buffer, pH 7.4, to be transferred rapidly to the specific binding sites on transferrin. Just as in the case of iron, this complexation requires the presence of a synergistic ion such as bicarbonate. The present system can be used to allow the binding of /sup 113/mIn to transferrin when coupled to an antibody. This method has been tested by studying the conjugation of an antibody, the IgG fraction of goat anti-rabbit-IgG, with either transferrin or desferoxamine, using glutaraldehyde as the coupling agent. Optimization in terms of total protein concentration and glutaraldehyde levels lead to products where the specific metal binding capacity of the transferrin moiety remains unchanged, and where the antibody retains 70% of its antigenic activity. The present system can be considered an extension of the ELISA techniques and can be used to determine, by a terminal /sup 113/mIn labeling technique, the level of specific binding of an antibody to its antigen.
Citation Formats
Gokce, A, Nakamura, R M, Tubis, M, and Wolf, W.
Synthesis of indium-labeled antibody-chelate conjugates for radioassays.
United Kingdom: N. p.,
1982.
Web.
doi:10.1016/0047-0740(82)90034-1.
Gokce, A, Nakamura, R M, Tubis, M, & Wolf, W.
Synthesis of indium-labeled antibody-chelate conjugates for radioassays.
United Kingdom.
https://doi.org/10.1016/0047-0740(82)90034-1
Gokce, A, Nakamura, R M, Tubis, M, and Wolf, W.
1982.
"Synthesis of indium-labeled antibody-chelate conjugates for radioassays."
United Kingdom.
https://doi.org/10.1016/0047-0740(82)90034-1.
@misc{etde_6857463,
title = {Synthesis of indium-labeled antibody-chelate conjugates for radioassays}
author = {Gokce, A, Nakamura, R M, Tubis, M, and Wolf, W}
abstractNote = {A method has been developed to achieve rapid and reproducible complexation of indium to transferrin at pH 7.4. The system consists of nitrilotriacetic acid (NTA) as the intermediate carrier ligand, whose function is to allow the /sup 113/m In ion, in a solution in Tris buffer, pH 7.4, to be transferred rapidly to the specific binding sites on transferrin. Just as in the case of iron, this complexation requires the presence of a synergistic ion such as bicarbonate. The present system can be used to allow the binding of /sup 113/mIn to transferrin when coupled to an antibody. This method has been tested by studying the conjugation of an antibody, the IgG fraction of goat anti-rabbit-IgG, with either transferrin or desferoxamine, using glutaraldehyde as the coupling agent. Optimization in terms of total protein concentration and glutaraldehyde levels lead to products where the specific metal binding capacity of the transferrin moiety remains unchanged, and where the antibody retains 70% of its antigenic activity. The present system can be considered an extension of the ELISA techniques and can be used to determine, by a terminal /sup 113/mIn labeling technique, the level of specific binding of an antibody to its antigen.}
doi = {10.1016/0047-0740(82)90034-1}
journal = []
volume = {9:2}
journal type = {AC}
place = {United Kingdom}
year = {1982}
month = {Jan}
}
title = {Synthesis of indium-labeled antibody-chelate conjugates for radioassays}
author = {Gokce, A, Nakamura, R M, Tubis, M, and Wolf, W}
abstractNote = {A method has been developed to achieve rapid and reproducible complexation of indium to transferrin at pH 7.4. The system consists of nitrilotriacetic acid (NTA) as the intermediate carrier ligand, whose function is to allow the /sup 113/m In ion, in a solution in Tris buffer, pH 7.4, to be transferred rapidly to the specific binding sites on transferrin. Just as in the case of iron, this complexation requires the presence of a synergistic ion such as bicarbonate. The present system can be used to allow the binding of /sup 113/mIn to transferrin when coupled to an antibody. This method has been tested by studying the conjugation of an antibody, the IgG fraction of goat anti-rabbit-IgG, with either transferrin or desferoxamine, using glutaraldehyde as the coupling agent. Optimization in terms of total protein concentration and glutaraldehyde levels lead to products where the specific metal binding capacity of the transferrin moiety remains unchanged, and where the antibody retains 70% of its antigenic activity. The present system can be considered an extension of the ELISA techniques and can be used to determine, by a terminal /sup 113/mIn labeling technique, the level of specific binding of an antibody to its antigen.}
doi = {10.1016/0047-0740(82)90034-1}
journal = []
volume = {9:2}
journal type = {AC}
place = {United Kingdom}
year = {1982}
month = {Jan}
}