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

Content Provider	Springer Nature Link
Author	Cao, Yongsheng Li, Di Cao, Chong Gao, Mingchun Zhang, Runxiang Ma, Bo Wang, Junwei
Copyright Year	2013
Abstract	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.
Starting Page	1441
Ending Page	1447
Page Count	7
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	35
Issue Number	9
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2013-05-21
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biological affinity C2 domain of streptococcal protein G Chicken IgY-binding ability Expression and purification Gene optimization Microbiology Biotechnology Applied Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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