Human müllerian inhibiting substance: enhanced purification imparts biochemical stability and restores antiproliferative effects.

Abstract:

:Separation of copurifying protease activity from recombinant human Müllerian inhibiting substance (rhMIS) bound to a monoclonal antibody immunoaffinity column by a high-salt wash results in cleaner preparations of rhMIS resistant to cleavage upon storage. In addition, an inhibitor of rhMIS antiproliferative activity is removed. Proteolytic cleavages produced by either a copurifying protease or exogenous plasmin occur at residues 229 and 427 but do not abolish rhMIS biological activity. This report details the modified immunoaffinity column isolation protocol suitable for proteins such as rhMIS and describes the biochemical and antiproliferative properties of this protein.

journal_name

Protein Expr Purif

authors

Ragin RC,Donahoe PK,Kenneally MK,Ahmad MF,MacLaughlin DT

doi

10.1016/1046-5928(92)90020-w

keywords:

subject

Has Abstract

pub_date

1992-06-01 00:00:00

pages

236-45

issue

3

eissn

1046-5928

issn

1096-0279

pii

1046-5928(92)90020-W

journal_volume

3

pub_type

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