Refolding of denatured/reduced lysozyme at high concentrations by artificial molecular chaperone-ion exchange chromatography

2010 ◽  
pp. NA-NA
Author(s):  
Chaozhan Wang ◽  
Qinming Zhang ◽  
Yan Cheng ◽  
Lili Wang
Keyword(s):  
Ion Exchange ◽  
Molecular Chaperone ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
High Concentrations

Highly concentrated single-chain atomic crystal LiMo3Se3 solution using ion-exchange chromatography

2018 ◽  
Vol 54 (88) ◽  
pp. 12503-12506 ◽  
Author(s):  
Sudong Chae ◽  
Seungbae Oh ◽  
Akhtar J. Siddiqa ◽  
Kyung Hwan Choi ◽  
Weon-Gyu Lee ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Aqueous Solutions ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Single Chain ◽  
Stern Layer ◽  
High Concentrations ◽  
Atomic Crystal

The enlargement of the Stern layer distance caused by this ion exchange improves the dispersibility of (Mo3Se3−)∞ chains and also prevents the re-bundling and aggregation of nanowires in aqueous solutions, even at high concentrations (1 mg mL−1).

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

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.

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