Modeling of complex antibody elution behavior under high protein load densities in ion exchange chromatography using an asymmetric activity coefficient

2017 ◽  
Vol 12 (3) ◽  
pp. 1600336 ◽  
Author(s):  
Thiemo C. Huuk ◽  
Tobias Hahn ◽  
Katharina Doninger ◽  
Jan Griesbach ◽  
Stefan Hepbildikler ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Activity Coefficient ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
High Protein ◽  
Elution Behavior ◽  
Protein Load

Isolation of 2-Acetamido-1-β-(L-β-Aspartamido)-1,2-Dideoxy-D-Glucose from Normal Human Urine

1972 ◽  
Vol 18 (9) ◽  
pp. 951-955 ◽  
Author(s):  
Barbara O’Neill Rowley ◽  
Paul B Hamilton
Keyword(s):  
Ion Exchange ◽  
Human Urine ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Individuals ◽  
Normal Human ◽  
Elution Behavior ◽  
Solvent Systems ◽  
And Migration ◽  
Layer Chromatography

Abstract A glycopeptide was isolated from normal human urine by fractionation on a column of Sephadex G-10 and preparative ion-exchange chromatography. Elution behavior during ion-exchange chromatography in two different solvent systems, amino acids formed upon hydrolysis, and migration on high-voltage electrophoresis and thin-layer chromatography were essentially identical for this substance and for authentic 2-acetamido-l-β-(L-β-aspartamido)-1,2-dideoxy-D-glucose. A technique was developed to permit analytical-scale fractionation of individual urines followed by analysis for this glycopeptide; urine from two normal individuals contained 7 and 11 µmol of 2-acetamido-1-β-(L-β-aspartamido)-1,2-dideoxy-D-glucose per liter.

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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