Characterization of the optimized C2 domain of protein G: finding its additional chicken IgY-binding ability

被引：1

作者：

Cao, Yongsheng ^{[1
]}

Li, Di ^{[1
]}

Cao, Chong ^{[1
]}

Gao, Mingchun ^{[1
]}

Zhang, Runxiang ^{[1
]}

Ma, Bo ^{[1
]}

Wang, Junwei ^{[1
]}

机构：

[1] Northeast Agr Univ, Coll Vet Med, Harbin 150030, Peoples R China

来源：

BIOTECHNOLOGY LETTERS | 2013年 / 35卷 / 09期

关键词：

Biological affinity; C2 domain of streptococcal protein G; Chicken IgY-binding ability; Expression and purification; Gene optimization; PURIFICATION; IMMUNOGLOBULINS; ANTIBODIES; CHROMATOGRAPHY; STREPTOCOCCUS; FRAGMENTS; ADSORBENT; COMPLEX; REAGENT; AUREUS;

D O I：

10.1007/s10529-013-1221-7

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The C2 domain of streptococcal protein G is a small (55 residue) peptide with immunoglobulin-binding activity. Following codon optimization, the gene was divided into four oligonucleotide fragments and amplified by overlap PCR. The recombinant plasmid pET30a-C2 was transformed into Escherichia coli Rosetta (DE3) PLysS for expression. After purification by Ni-NTA, the fusion protein was identified by western-blotting, Dot-ELISA and ELISA. His-tagged C2 bound to human, rabbit, cattle, pig, goat, mouse or guinea pig IgG had no affinity for goose, duck, wild duck, wild turkey and red-crowned crane IgY. Its affinity for chicken IgY, however, was comparable to that of guinea pig IgG. The C2 domain may therefore provide an ideal material for the purification and detection of immunoglobulin G from various mammals.

引用

页码：1441 / 1447

页数：7

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