scholarly journals Mathematical modeling of elution curves for a protein mixture in ion exchange chromatography applied to high protein concentration

2009 ◽  
Vol 104 (3) ◽  
pp. 572-581 ◽  
Author(s):  
C.A. Orellana ◽  
C. Shene ◽  
J.A. Asenjo
Keyword(s):  
Mathematical Modeling ◽  
Ion Exchange ◽  
Protein Concentration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
High Protein ◽  
Protein Mixture ◽  
High Protein Concentration ◽  
Elution Curves

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

scholarly journals Investigation of isolation conditions and ion-exchange purification of protein coagulation components from common bean seed

2007 ◽  
pp. 3-10
Author(s):  
Mirjana Antov ◽  
Marina Sciban ◽  
Slavica Adamovic ◽  
Mile Klasnja
Keyword(s):  
Ion Exchange ◽  
Common Bean ◽  
Crude Extract ◽  
Protein Concentration ◽  
Extraction Procedure ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Bean Seed ◽  
Coagulation Activity ◽  
Water As Solvent

Investigation of an extraction procedure of protein coagulants from common bean seed regarding concentration of NaCl and pH was performed. High values of protein concentration and coagulation activity in crude extract (9.19 g/l and 23.9%, respectively) were obtained when the extraction was performed using 0.5 mol/l NaCl and water as solvent, which represents an advantage for economic and environmental reasons. Crude extract of common bean seed was purified by precipitation at two different percentages of (NH4)2SO4 saturation, followed by batch ion-exchange chromatography. The highest obtained coagulation activity, 45%, was determined in fraction that was eluated at 1.75 mol/l NaCl from resin loaded with proteins precipitated upon 80-100% (NH4)2SO4 saturation. High values of coagulation activity showed by some eluates suggest their application as natural coagulant for water purification. .

scholarly journals Interaction between S-Type Pyocins and Microcin-II-Like Bacteriocins in Pseudomonas aeruginosa

2021 ◽  
Vol 83 (3) ◽  
pp. 72-80
Author(s):  
O.B. Balko ◽  
Keyword(s):  
Molecular Weight ◽  
Pseudomonas Aeruginosa ◽  
Ion Exchange ◽  
Protein Concentration ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Activity Increase ◽  
Activity Indices

According to our previous results, S-type bacteriocins of Pseudomonas aeruginosa are characterized by high activity against phytopathogenic Pseudomonas syringae strains. In addition to these pyocins producing strains are able to synthesize microcin-II-like bacteriocins. Presence of interaction between these two killer factors can determine methods of their use and activity increase of bacteriocins with antiphytopathogenic properties. The aim of the work was to test possibility of interaction between S-type pyocins and microcin-II-like bacteriocins of P. aeruginosa. Methods. The objects of the study were pyocins produced by 6 P. aeruginosa strains. Killer factors in composition of induced lysates were concentrated by 70% ammonium sulphate precipitation, dialyzed through dialysis membrane with molecular weight cut-off (MWCO) 3.5 kDa. Then ion-exchange chromatography with DEAE-cellulose, gel filtration with Sephadex G-75 and ultracentrifugation at 215.000 g for 1 and 4 hours were used for their separation. Protein concentration and antimicrobial activity were determined in obtained fractions. Visualization of proteins in active fraction composition was conducted by electrophoresis according to the Laemmli method. Results. Under ion-exchange chromatography with DEAE-cellulose application elution of bacteriocins available in lysate composition occurs simultaneously. The highest indices of activity and protein concentration were in the 4th fraction, containing two protein bands with molecular weight near 58 and 9 kDa, which are typical for S5 pyocin and microcin-II-like bacteriocins of P. aeruginosa. Further gel filtration of sampled fractions through Sephadex G-75 allowed to separate noted killer factors and obtaine purified fraction containing microcin-II-like pyocins only. Application of ultracentrifugation during 1 hour didn’t precipitate studied bacteriocins, whereas during 4 hours – lead to their separation. At the same time a twofold increase of activity indices for S-type pyocins in precipitates and for microcin-IIlike killer factors – in supernatants were observed. However achieved concentration was characterized by short-term effect, since in 14 days activity of supernatants decreased by 4–16 times, and for precipitates – by 80–640 times. Then revealed tendency for activity decrease continued. Conclusions. S-type pyocins and microcin-II-like bacteriocins of P. aeruginosa interact with each other, that ensures their stabilization and protects again destruction. Application of methods that cause separation of these killer factors is inexpedient, since it results into considerable decrease of bacteriocin activity indices.

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.

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