DEVELOPMENT OF ANTIBODIES TO UNPROTECTED GLYCOSYLATION SITES ON RECOMBINANT HUMAN GM-CSF

被引：168

作者：

GRIBBEN, JG ^{[1
]}

DEVEREUX, S ^{[1
]}

THOMAS, NSB ^{[1
]}

KEIM, M ^{[1
]}

JONES, HM ^{[1
]}

GOLDSTONE, AH ^{[1
]}

LINCH, DC ^{[1
]}

机构：

[1] UNIV COLL & MIDDLESEX SCH MED,FAC CLIN SCI,DEPT HAEMATOL,LONDON WC1E 6HX,ENGLAND

来源：

LANCET | 1990年 / 335卷 / 8687期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/0140-6736(90)90665-R

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

In 4 out of 16 patients receiving recombinant human granulocyte macrophage colony stimulating factor (rhGM-CSF) in phase I/II studies antibodies developed to the recombinant protein. The antibodies react with sites on the native protein backbone which are normally protected by O-linked glycosylation but which are exposed in rhGM-CSF produced in yeast and Escherichia coli. Antigenicity of recombinant human proteins due to non glycosylation may have relevance to the choice of host system for production of factors for clinical use. © 1990.

引用

页码：434 / 437

页数：4

共 13 条

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