A Safety Study of Albumex® 5, a Human Albumin Solution Produced by Ion Exchange Chromatography

Vox Sanguinis ◽  
1996 ◽  
Vol 70 (4) ◽  
pp. 198-202
Author(s):  
M. Wolf ◽  
H. Kronenberg ◽  
A. Dodds ◽  
P. Miach ◽  
J. Isbister ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Human Albumin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Albumin Solution ◽  
Safety Study ◽  
Human Albumin Solution

A Safety Study of Albumex®5, a Human Albumin Solution Produced by Ion Exchange Chromatography

Vox Sanguinis ◽  
1996 ◽  
Vol 70 (4) ◽  
pp. 198-202 ◽  
Author(s):  
M. Wolf ◽  
H. Kronenberg ◽  
A. Dodds ◽  
P. Miach ◽  
J. Isbister ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Human Albumin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Albumin Solution ◽  
Safety Study ◽  
Human Albumin Solution

Prekallikrein Activator in Human Albumin Prepared by Cold-Ethanol Precipitation Methods and by ION Exchange Chromatography

1979 ◽  
Author(s):  
M.S. Horowitz ◽  
B. Horowitz
Keyword(s):  
Ion Exchange ◽  
Ph Control ◽  
Human Albumin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Efficient Removal ◽  
Plasma Fractions ◽  
Plasma Protein Fraction ◽  
Acids And Bases ◽  
Strong Acids

Hypotensive reactions associated with the administration of albumin-containing plasma fractions have been attributed by Alving et al. to the presence of Hageman-factor fragments or prekallikrein activator (PKA). Using a radiochemical assay which measures kallikrein activation, we have investigated the PKA content of plasma fractions prepared according to the cold-ethanol method 6 of Cohn et al., several modified cold-ethanol procedures, and the ion-exchange chromatography system of Curling et al. Cohn fraction IV-4 contains both PKA and a precursor from which PKA activity can be generated by kaolin treatment, while Cohn Fraction V is free of both of these entities. Modification of Cohn method 6 by combining the IV-1 and IV-4 precipitation steps results in less efficient removal of PKA, especially when strong acids and bases replace acetate buffers for pH control. Prekal1ikrein activator activity accompanies albumin throughout the ion-exchange purification procedure and is present in the final albumin product prepared by this method. These results explain why PKA occurs frequently in the derivative known as plasma protein fraction and rarely in albumin which has been made according to Cohn method 6.

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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