Separation of acidic peptides by reversed-phase ion-pair chromatography. Analytical application to a series of acidic substrates of casein kinases.
J Chromatogr
; 548(1-2): 329-34, 1991 Jul 12.
Article
em En
| MEDLINE
| ID: mdl-1939431
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Proteínas Quinases
Limite:
Animals
Idioma:
En
Revista:
J Chromatogr
Ano de publicação:
1991
Tipo de documento:
Article