Characterization of a recombinant granzyme B derivative as a "restriction" protease

被引：2

作者：

Fynbo, CH

Lorentsen, RH

Etzerodt, M

Thogersen, HC

Holtet, TL

机构：

[1] Aarhus Univ, Dept Mol Biol, DK-8000 Aarhus C, Denmark

[2] Borean Pharma AS, DK-8000 Aarhus C, Denmark

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2005年 / 39卷 / 02期

关键词：

recombinant serine protease; granzyme B; hydrolytic activity; proteolytic activity; stability;

D O I：

10.1016/j.pep.2004.10.010

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Blood coagulation factor X-a (FXa) and Thrombin are well-known serine proteases often used for processing of recombinant fusion proteins., but because they are purified from bovine blood or other animal sources. there is a risk of pathogenic contaminants in the preparation of the proteases. We report here the characterization of a recombinant serine protease produced in Escherichia coli, which can be used as a specific and efficient alternative to FXa, and Thrombin as processing protease. This recombinant protease is derived from human granzyme B (GrB). The protease is found to be very stable in general. and it performs very well in the cleavage of several different fusion proteins tested and was even found superior to processing by FXa, in two cases. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：209 / 218

页数：10

共 28 条

[11] Determination of the P′1, P′2 and P′3 subsite-specificity of factor Xa [J].