Ion-exchange chromatography has been used to separate amino acids since 1956. 1 These early separations are comparable to classical column chromatography on silica or alumina as regards both expenditure and output. The resins or gels used were relatively coarse, pressures were low and the chromatogr
Micropreparative ion exchange high performance liquid chromatography: Applications to microsequence analysis
β Scribed by E. C. Nice; L. Fabri; A. Hammacher; K. Andersson; U. Hellman
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 757 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0269-3879
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β¦ Synopsis
Abstract
Data on the characterization of anion and cation micropreparative (50X1.6 mm i.d.) HPLC columns is presented. It is shown how subnanomole quantities of protein can be efficiently recovered from such columns, rendering them compatible for use in multidimensional chromatographic strategies for the purification of trace biological samples. By selection of appropriate solvent systems (e.g., bufferβfree sodium chloride solutions), the small eluant peak volumes can be loaded directly onto the gas phase sequencer, and Nβterminal sequence data obtained. The potential of the technique is illustrated for the purification of a GTPase activating protein (GAPβ3).
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## Abstract Silver ion chromatography, utilizing two commercially available HPLC columns connected in series, was used to separate a variety of triacylglycerol positional isomers. The isomers had a fatty acid composition of ABA and AAB, where A and B were fatty acids containing zero to three double