Abstract
A simple method is described for affinity purification of radiolabeled antibodies using glutaraldehyde-fixed tumor target cells. The cell-bound antibody fraction is removed from the cells by an acid wash and then immediately subjected to buffer-exchange chromatography. The method was applied to the D3 murine monoclonal antibody which binds to a 290 kDa antigen on the surface of Line 10 guinea pig carcinoma cells. No alteration in the molecular size profile was detected after acid washing. Purification resulted in a significant increase in immunoreactivity by an average of 14 [+-] 47% (SD; range 4-30%). (author).
Juweid, M;
Sato, J;
Paik, C;
Onay-Basaran, S;
Weinstein, J N;
Neumann, R D
[1]
- National Cancer Inst., Bethesda, MD (United States)
Citation Formats
Juweid, M, Sato, J, Paik, C, Onay-Basaran, S, Weinstein, J N, and Neumann, R D.
A simple method for affinity purification of radiolabeled monoclonal antibodies.
United Kingdom: N. p.,
1993.
Web.
Juweid, M, Sato, J, Paik, C, Onay-Basaran, S, Weinstein, J N, & Neumann, R D.
A simple method for affinity purification of radiolabeled monoclonal antibodies.
United Kingdom.
Juweid, M, Sato, J, Paik, C, Onay-Basaran, S, Weinstein, J N, and Neumann, R D.
1993.
"A simple method for affinity purification of radiolabeled monoclonal antibodies."
United Kingdom.
@misc{etde_6077280,
title = {A simple method for affinity purification of radiolabeled monoclonal antibodies}
author = {Juweid, M, Sato, J, Paik, C, Onay-Basaran, S, Weinstein, J N, and Neumann, R D}
abstractNote = {A simple method is described for affinity purification of radiolabeled antibodies using glutaraldehyde-fixed tumor target cells. The cell-bound antibody fraction is removed from the cells by an acid wash and then immediately subjected to buffer-exchange chromatography. The method was applied to the D3 murine monoclonal antibody which binds to a 290 kDa antigen on the surface of Line 10 guinea pig carcinoma cells. No alteration in the molecular size profile was detected after acid washing. Purification resulted in a significant increase in immunoreactivity by an average of 14 [+-] 47% (SD; range 4-30%). (author).}
journal = []
volume = {20:3}
journal type = {AC}
place = {United Kingdom}
year = {1993}
month = {Apr}
}
title = {A simple method for affinity purification of radiolabeled monoclonal antibodies}
author = {Juweid, M, Sato, J, Paik, C, Onay-Basaran, S, Weinstein, J N, and Neumann, R D}
abstractNote = {A simple method is described for affinity purification of radiolabeled antibodies using glutaraldehyde-fixed tumor target cells. The cell-bound antibody fraction is removed from the cells by an acid wash and then immediately subjected to buffer-exchange chromatography. The method was applied to the D3 murine monoclonal antibody which binds to a 290 kDa antigen on the surface of Line 10 guinea pig carcinoma cells. No alteration in the molecular size profile was detected after acid washing. Purification resulted in a significant increase in immunoreactivity by an average of 14 [+-] 47% (SD; range 4-30%). (author).}
journal = []
volume = {20:3}
journal type = {AC}
place = {United Kingdom}
year = {1993}
month = {Apr}
}