EXPRESSION AND PURIFICATION OF BIOLOGICALLY-ACTIVE DOMAIN-I OF THE HUMAN POLYMERIC IMMUNOGLOBULIN RECEPTOR

被引：22

作者：

BAKOS, MA ^{[1
]}

WIDEN, SG ^{[1
]}

GOLDBLUM, RM ^{[1
]}

机构：

[1] UNIV TEXAS,MED BRANCH,SEALY CTR MOLEC SCI,GALVESTON,TX 77555

来源：

MOLECULAR IMMUNOLOGY | 1994年 / 31卷 / 02期

关键词：

D O I：

10.1016/0161-5890(94)90088-4

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：

Previous studies using proteolytic fragments and synthetic peptides have indicated that domain I of human polymeric immunoglobulin receptor (PIgR) is necessary for ligand binding. The expression in E. coli, and subsequent IgM-affinity purification of domain I of human PIgR is described. The recombinant domain I protein (rDI) was similar in structure to native SC domain I in that it bound specifically to MAb 6G11, an antibody which recognizes a critical portion of the Pig binding site in domain I. The biological activity of rDI was indicated by high affinity binding to PIgA (Kd = 1.6 X 10(-7) M) and IgM (Kd = 5.1 X 10(-7) M). Domain I of human SC is therefore sufficient for binding to Pig.

引用

页码：165 / 168

页数：4

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