Immunoglobulin-binding protein-based affinity chromatography in bispecific antibody purification: Functions beyond product capture

2021 ◽  
Vol 188 ◽  
pp. 105976
Author(s):  
Yifeng Li
Vaccine ◽  
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Vol 30 (30) ◽  
pp. 4578
Author(s):  
Roger S. Geertsema ◽  
Carolyn Worby ◽  
Robert P. Kruger ◽  
Yuichi Tagawa ◽  
Riccardo Russo ◽  
...  

2007 ◽  
Vol 44 (16) ◽  
pp. 3982 ◽  
Author(s):  
Julia Burman ◽  
Elisa Leung ◽  
David E. Isenman ◽  
Jean M.H. van den Elsen

1991 ◽  
Vol 3 (5) ◽  
pp. 483-496 ◽  
Author(s):  
E B Fontes ◽  
B B Shank ◽  
R L Wrobel ◽  
S P Moose ◽  
G R OBrian ◽  
...  

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Vol 71 (10) ◽  
pp. 6079-6082 ◽  
Author(s):  
Tara C. Smith ◽  
Darren D. Sledjeski ◽  
Michael D. P. Boyle

ABSTRACT Streptococcus pyogenes protein H (sph) is an immunoglobulin-binding protein present in the Mga regulon of certain M1 serotype isolates. Although sph is present in many strains, it is frequently not expressed. In this paper we show that protein H was highly expressed after bacteria were injected into the skin of mice and were recovered from the blood, kidney, or spleen at various times postinfection. The percentage of protein H-positive colonies increased with time, reaching 100% in the spleen and kidney within 24 to 72 h postinfection. The up-regulation of sph expression was also observed in a mga mutant.


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