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
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
收藏
页码:224 / 230
页数:7
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