HUMAN MULLERIAN INHIBITING SUBSTANCE - ENHANCED PURIFICATION IMPARTS BIOCHEMICAL STABILITY AND RESTORES ANTIPROLIFERATIVE EFFECTS

被引：60

作者：

RAGIN, RC

DONAHOE, PK

KENNEALLY, MK

AHMAD, MF

MACLAUGHLIN, DT

机构：

[1] MASSACHUSETTS GEN HOSP, DIABET UNIT, BOSTON, MA 02114 USA

[2] HARVARD UNIV, SCH MED, DEPT SURG & MED, BOSTON, MA 02115 USA

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1992年 / 3卷 / 03期

关键词：

D O I：

10.1016/1046-5928(92)90020-W

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 anti-proliferative properties of this protein. © 1992.

引用

页码：236 / 245

页数：10

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