Purification of IgG Using Protein A or Protein G

Author(s):  
Mark Page ◽  
Robin Thorpe
Keyword(s):  
2003 ◽  
Vol 31 (3) ◽  
pp. 716-718 ◽  
Author(s):  
N.G. Housden ◽  
S. Harrison ◽  
S.E. Roberts ◽  
J.A. Beckingham ◽  
M. Graille ◽  
...  

Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A (Staphylococcus aureus) and Protein G (Streptococcus). Both of these proteins bind predominantly to the interface of CH2-CH3 heavy chains, while Protein L binds exclusively to the VL domain of the κ-chain. The function of these proteins in vivo is not clear but it is thought that they enable the bacteria to evade the host's immune system. Two binding sites for κ-chain on a single Ig-binding domain from Protein L have recently been reported and we give evidence that one site has a 25–55-fold higher affinity for κ-chain than the second site.


mAbs ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 1464-1478 ◽  
Author(s):  
Romain Ollier ◽  
Paul Wassmann ◽  
Thierry Monney ◽  
Christelle Ries Fecourt ◽  
Sunitha Gn ◽  
...  

2008 ◽  
Vol 870 (1) ◽  
pp. 55-62 ◽  
Author(s):  
Georgeen Gaza-Bulseco ◽  
Sagar Faldu ◽  
Karen Hurkmans ◽  
Chris Chumsae ◽  
Hongcheng Liu

1991 ◽  
Vol 145 (1-2) ◽  
pp. 255-258 ◽  
Author(s):  
Zhikang Peng ◽  
F. Estelle ◽  
R. Simons ◽  
Allan B. Becker

2019 ◽  
Vol 2019 (1) ◽  
pp. pdb.prot099143 ◽  
Author(s):  
Jordan B. Fishman ◽  
Eric A. Berg
Keyword(s):  

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