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Separation of basic, hydrophilic peptides by reversed-phase ion-pair chromatography: I. Analytical applications with particular reference to a class of serine peptide substrates of cyclic AMP-stimulated protein kinase by B. Fransson; U. Ragnarsson; Ö. Zetterqvist is a Chemistry article available to read on EtoBox.

What is Separation of basic, hydrophilic peptides by reversed-phase ion-pair chromatography: I. Analytical applications with particular reference to a class of serine peptide substrates of cyclic AMP-stimulated protein kinase about?

Basic, hydrophilic peptides exemplified by Arg-Arg-Ala-Ser-Val, a substrate of cyclic AMP-stimulated protein kinase, could be efficiently retarded by ion-pair formation with n-hexanesulphonic acid on a C18 column in phosphate buffer systems with ethanol as organic modifier. Reversed-phase ion-pair chromatography appears to be an ideal method for separating peptides of this type. Highly efficient separations under isocratic conditions are reported for peptides composed of 5-9 amino acids, with up to three basic residues, most having sequences derived from the phosphor, ylatable site of pyruvate kinase.

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Author

B. Fransson; U. Ragnarsson; Ö. Zetterqvist

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1873-3778)

Published

1982

Language

EN

Field

Chemistry (Physical Sciences)