A simple method for affinity purification of radiolabeled monoclonal antibodies

Malik Juweid; Jun Sato; Chang Paik; Sema Onay-Basaran; John N. Weinstein; Ronald D. Neumann

doi:10.1016/0969-8051(93)90053-W

A simple method for affinity purification of radiolabeled monoclonal antibodies

Malik Juweid, Jun Sato, Chang Paik, Sema Onay-Basaran, John N. Weinstein, Ronald D. Neumann

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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%).

Original language	English (US)
Pages (from-to)	311-315
Number of pages	5
Journal	Nuclear Medicine and Biology
Volume	20
Issue number	3
DOIs	https://doi.org/10.1016/0969-8051(93)90053-W
State	Published - Apr 1993
Externally published	Yes

ASJC Scopus subject areas

Molecular Medicine
Radiology Nuclear Medicine and imaging
Cancer Research

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10.1016/0969-8051(93)90053-W

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title = "A simple method for affinity purification of radiolabeled monoclonal antibodies",

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 = "Malik Juweid and Jun Sato and Chang Paik and Sema Onay-Basaran and Weinstein, {John N.} and Neumann, {Ronald D.}",

year = "1993",

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T1 - A simple method for affinity purification of radiolabeled monoclonal antibodies

AU - Juweid, Malik

AU - Sato, Jun

AU - Paik, Chang

AU - Onay-Basaran, Sema

AU - Weinstein, John N.

AU - Neumann, Ronald D.

PY - 1993/4

Y1 - 1993/4

N2 - 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%).

AB - 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%).

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JO - Nuclear Medicine and Biology

JF - Nuclear Medicine and Biology

IS - 3

ER -

A simple method for affinity purification of radiolabeled monoclonal antibodies

Abstract

ASJC Scopus subject areas

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