Fully automated micro- and nanoscale one- or two-dimensional high-performance liquid chromatography system for liquid chromatography–mass spectrometry compatible with non-volatile salts for ion exchange chromatography

2005 ◽  
Vol 1063 (1-2) ◽  
pp. 57-69 ◽  
Author(s):  
Junichi Masuda ◽  
Dawn M. Maynard ◽  
Masayuki Nishimura ◽  
Teruhisa Ueda ◽  
Jeffrey A. Kowalak ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Ion Exchange ◽  
High Performance ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Two Dimensional ◽  
Liquid Chromatography Mass Spectrometry ◽  
Liquid Chromatography System

Quantitation of o- and p-Sulfamoylbenzoic Acids in Commercial Saccharin by High-Performance Liquid Chromatography

1976 ◽  
Vol 59 (2) ◽  
pp. 243-250
Author(s):  
James J Nelson
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Ion Exchange ◽  
Sodium Salt ◽  
Mobile Phase ◽  
High Performance ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Anion Exchange Column ◽  
Para Isomer

Abstract Quantitation of o- and p-sulfamoylbenzoic acid residues in saccharin and its sodium salt is achieved by a method comprising methanolic extraction and high-performance ion exchange chromatography. A commercially available anion exchange column was employed with an aqueous buffered (pH 9.2) mobile phase. As little as 80 ppm of the ortho-isomer and 25 ppm of the para-isomer can be accurately determined. The levels of detectability (2 times noise) are estimated as 8 ppm (0.16 μg on column) and 2.5 ppm (0.05 μg on column), respectively. Recoveries from saccharin ranged from 92.7 to 96.5% (ortho) and from 92.2 to 103.3% (para). Recoveries from the sodium salt ranged from 93.1 to 104.4% (ortho) and from 93.5 to 97.8% (para). Of 9 other potential saccharin impurities tested separately, only one was found to interfere slightly in the chromatographic part of the procedure.

Ion-exchange high-performance liquid-chromatography steps in peptide purifications

1982 ◽  
Vol 2 (10) ◽  
pp. 803-811 ◽  
Author(s):  
Hedvig Von Bahr-Lindstróm ◽  
Ulla Moberg ◽  
Jórgen Sjódahl ◽  
Hans Jórnvall
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Ion Exchange ◽  
High Speed ◽  
High Performance ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Reverse Phase ◽  
Complete Purification ◽  
Ion Exchange Hplc

Ion-exchange high-performance liquid chromatography (HPLC; on Ultropac TSK DEAE and CM) is compared with conventional soft-gel ion-exchange chromatography in identical peptide purifications. The results show that separating properties are similar, but as expected, ion-exchange HPLC has a much higher resolving capacity and a higher sensitivity, and allows a considerably shorter total separation time. The same buffer systems as for conventional ion-exchange chromatography can be used, including urea to solubilize large peptides, if care is taken not to exceed the pH limits set by the column matrix. A complete purification scheme by HPLC in the nanomolar range, utilizing exclusion, ion-exchange, and reverse-phase chromatographies, is given with a complex peptide mixture from a digest of a large protein. Similar steps as in conventional soft-gel schemes can be utilized. It is concluded that ion-exchange HPLC is a suitable complement to commonly used reverse-phase HPLC steps and that it permits high speed and sensitivity over wide ranges of peptide sizes and amounts.

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