Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1991-12-17
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
548
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
329-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Separation of acidic peptides by reversed-phase ion-pair chromatography. Analytical application to a series of acidic substrates of casein kinases.
pubmed:affiliation
Department of Organic Chemistry of University of Padova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't