scholarly journals Laboratory studies of /sup 235/U enrichment by chemical separation methods. [Ion exchange, electrodialysis, gas exchange chromatography]

1976 ◽  
Author(s):  
P. Daloisi ◽  
M. Orlett ◽  
J. Tracy ◽  
A. Saraceno
Keyword(s):  
Gas Exchange ◽  
Ion Exchange ◽  
Chemical Separation ◽  
Exchange Chromatography ◽  
Laboratory Studies

scholarly journals A rapid and efficient ion-exchange chromatography for Lu–Hf, Sm–Nd, and Rb–Sr geochronology and the routine isotope analysis of sub-ng amounts of Hf by MC-ICP-MS

2015 ◽  
Vol 30 (11) ◽  
pp. 2323-2333 ◽  
Author(s):  
R. Bast ◽  
E. E. Scherer ◽  
P. Sprung ◽  
M. Fischer-Gödde ◽  
A. Stracke ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Isotope Analysis ◽  
Chemical Separation ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Separation Technique ◽  
Small Samples ◽  
Icp Ms

We present an effective chemical separation technique for Lu–Hf geochronology on small samples (sub-ng range Hf) and precise 176Hf/177Hf analysis.

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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