Separation of acidic peptides by reversed-phase ion-pair chromatography. Analytical application to a series of acidic substrates of casein kinases.
A series of small peptides including clusters of glutamyl residues, synthesized to study the site specificity of rat liver (L-CK2) and yeast (Y-CK2) casein kinase-2, are analytically characterized by ion-pair high-performance liquid chromatography using tetrabutylammonium as counter-ion and acetonitrile as modifier of the aqueous phase. Under these conditions peptides of slightly different acidity can be separated and the elution order parallels the hydrophobicity of the ion-pair-peptide complexes, which increases with the number of the acidic functions present in the sequence.
Department of Organic Chemistry of University of Padova, Italy.
A
A
Calderan
P
P
Ruzza
O
O
Marin
M
M
Secchieri
G
G
Borin
F
F
Marchiori
D000595:Amino Acid Sequence; D000818:Animals; D047388:Casein Kinases; D002851:Chromatography, High Pressure Liquid; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification*; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D010455:Peptides; D011494:Protein Kinases; D047388:Casein Kinases