scholarly journals Real-time Monitoring of Intermediates Reveals the Reaction Pathway in the Thiol-Disulfide Exchange between Disulfide Bond Formation Protein A (DsbA) and B (DsbB) on a Membrane-immobilized Quartz Crystal Microbalance (QCM) System

2013 ◽  
Vol 288 (50) ◽  
pp. 35969-35981 ◽  
Author(s):  
Kenjiro Yazawa ◽  
Hiroyuki Furusawa ◽  
Yoshio Okahata
Keyword(s):  
Real Time ◽  
Quartz Crystal Microbalance ◽  
Disulfide Bond ◽  
Quartz Crystal ◽  
Reaction Pathway ◽  
Bond Formation ◽  
Protein A ◽  
Disulfide Bond Formation ◽  
Real Time Monitoring ◽  
Disulfide Exchange

scholarly journals Two Pairs of Conserved Cysteines Are Required for the Oxidative Activity of Ero1p in Protein Disulfide Bond Formation in the Endoplasmic Reticulum

2000 ◽  
Vol 11 (9) ◽  
pp. 2833-2843 ◽  
Author(s):  
Alison R. Frand ◽  
Chris A. Kaiser
Keyword(s):  
Endoplasmic Reticulum ◽  
Disulfide Bond ◽  
Mutational Analysis ◽  
Bond Formation ◽  
Secretory Proteins ◽  
Disulfide Bond Formation ◽  
Major Pathway ◽  
Disulfide Exchange ◽  
Redox Active ◽  
Protein Disulfide

In the major pathway for protein disulfide-bond formation in the endoplasmic reticulum (ER), oxidizing equivalents flow from the conserved ER-membrane protein Ero1p to secretory proteins via protein disulfide isomerase (PDI). Herein, a mutational analysis of the yeast ERO1 gene identifies two pairs of conserved cysteines likely to form redox-active disulfide bonds in Ero1p. Cys100, Cys105, Cys352, and Cys355 of Ero1p are important for oxidative protein folding and for cell viability, whereas Cys90, Cys208, and Cys349 are dispensable for these functions. Substitution of Cys100 with alanine impedes the capture of Ero1p-Pdi1p mixed-disulfide complexes from yeast, and also blocks oxidation of Pdi1p in vivo. Cys352 and Cys355 are required to maintain the fully oxidized redox state of Ero1p, and also play an auxiliary role in thiol–disulfide exchange with Pdi1p. These results suggest a model for the function of Ero1p wherein Cys100 and Cys105 form a redox-active disulfide bond that engages directly in thiol–disulfide exchange with ER oxidoreductases. The Cys352–Cys355 disulfide could then serve to reoxidize the Cys100–Cys105 cysteine pair, possibly through an intramolecular thiol–disulfide exchange reaction.

scholarly journals On-column disulfide bond formation of monoclonal antibodies during Protein A chromatography eliminates low molecular weight species and rescues reduced antibodies

mAbs ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 1829333
Author(s):  
Zhijun Tan ◽  
Vivekh Ehamparanathan ◽  
Tingwei Ren ◽  
Peifeng Tang ◽  
Laurel Hoffman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Protein A ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation

Real-time monitoring of the cell agglutination process with a quartz crystal microbalance

2008 ◽  
Vol 383 (1) ◽  
pp. 130-136 ◽  
Author(s):  
Liang Tan ◽  
Xue’en Jia ◽  
Xiangfu Jiang ◽  
Youyu Zhang ◽  
Hao Tang ◽  
...  
Keyword(s):  
Real Time ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Real Time Monitoring ◽  
Cell Agglutination
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