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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%).

journal_name

Nucl Med Biol

journal_title

Nuclear medicine and biology

authors

Juweid M,Sato J,Paik C,Onay-Basaran S,Weinstein JN,Neumann RD

doi

10.1016/0969-8051(93)90053-w

subject

Has Abstract

pub_date

1993-04-01 00:00:00

pages

311-5

issue

3

eissn

0969-8051

issn

1872-9614

pii

0969-8051(93)90053-W

journal_volume

20

pub_type

杂志文章

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