Unfolding and Refolding of Disulfide Proteins Using the Method Disulfide Scrambling

2011 ◽  
pp. 91-108
Author(s):  
Rowen J. Y. Chang
Keyword(s):  
2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.


2016 ◽  
Vol 1864 (9) ◽  
pp. 1188-1194 ◽  
Author(s):  
Wang-Chou Sung ◽  
Chiung-Wen Chang ◽  
Sheng-Yu Huang ◽  
Ting-Yu Wei ◽  
Yi-Li Huang ◽  
...  

1986 ◽  
Vol 155 (1) ◽  
pp. 123-128 ◽  
Author(s):  
Jeffrey L. Browning ◽  
Robert J. Mattaliano ◽  
E.Pingchang Chow ◽  
Shu-Mei Liang ◽  
Bernard Allet ◽  
...  

2009 ◽  
Vol 28 (6) ◽  
pp. 300-304 ◽  
Author(s):  
Jui-Yoa Chang ◽  
Bao-Yuan Lu ◽  
Li Li
Keyword(s):  

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