HIGH-LEVEL PRODUCTION OF MURINE INTERLEUKIN-5 (IL-5) UTILIZING RECOMBINANT BACULOVIRUS EXPRESSION - PURIFICATION OF THE RIL-5 AND ITS USE IN ASSESSING THE BIOLOGIC ROLE OF IL-5 GLYCOSYLATION

被引：21

作者：

KUNIMOTO, DY

ALLISON, KC

WATSON, C

FUERST, T

ARMSTRONG, GD

PAUL, W

STROBER, W

机构：

[1] NIAID,IMMUNOL LAB,BETHESDA,MD 20892

[2] UNIV ALBERTA,DEPT MED,EDMONTON T6G 2E1,ALBERTA,CANADA

[3] NIAID,CLIN INVEST LAB,MUCOSAL IMMUN SECT,BETHESDA,MD 20892

[4] NIAID,BIOCHEM LAB,BETHESDA,MD 20892

来源：

CYTOKINE | 1991年 / 3卷 / 03期

关键词：

IL-5; BACULOVIRUS; RECOMBINANT; MURINE; GLYCOSYLATION;

D O I：

10.1016/1043-4666(91)90020-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We describe here a recombinant baculovirus expression system useful for high level production of murine recombinant interleukin-5 (rIL-5). In addition, we describe a single-step technique of purification of the rIL-5 from the baculovirus-infected Sf9 cell supernatants, using an anti-IL-5 affinity column. The baculovirus-derived rIL-5 has physical properties and functional activities in various lymphoid cell assays similar to those of natural T cell-derived IL-5 and reacts with anti-IL-5 antibodies. Finally, the rIL-5 is similar to natural T cell-derived IL-5 in manifesting heterogeneous glycosylation; however, glycosylation does not appear to be necessary for biologic function, at least in a lymphoid cell proliferation assay. © 1991.

引用

页码：224 / 230

页数：7

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