Advances in gentle immunoaffinity chromatography.

Abstract:

:Immunoaffinity chromatography is one of the most powerful fractionation steps available for protein purification; however, it is often difficult to elute bound protein without using harsh or denaturing elution conditions. The development of methods to identify monoclonal antibodies that bind antigens tightly, but release under gentle, non-denaturing conditions has made possible the immunoaffinity purification of labile, multisubunit enzyme complexes with high yield and high specific activity. This work has implications for emerging proteomic applications, allowing identification of new protein-protein interaction partners, retention of biological activity and the isolation of protein complexes more amenable to crystallization and structure determination.

journal_name

Curr Opin Biotechnol

authors

Burgess RR,Thompson NE

doi

10.1016/s0958-1669(02)00340-3

subject

Has Abstract

pub_date

2002-08-01 00:00:00

pages

304-8

issue

4

eissn

0958-1669

issn

1879-0429

pii

S0958166902003403

journal_volume

13

pub_type

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