Linked Life Data

15536629

Source:http://linkedlifedata.com/resource/pubmed/id/15536629

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2004-11-23
pubmed:abstractText
Monovalent cations often associate with peptides and proteins under mass spectrometry (MS) conditions, resulting in a discernable, but often misleading, adduct cluster pattern. These adduct cluster peaks reduce the signal intensity of specific peptide species by splitting the ion population into multiple mass peaks, suppressing the ionization of neighboring low-abundance peaks, and interfering with identification of post-translational modifications. Further, monovalent contaminants tend to form a distribution of matrix cluster peaks in matrix-associated laser desorption/ionization time-of-flight (MALDI-TOF) spectra causing interference and suppression in the mass range below 1400 Da. The most common method for reduction or elimination of adduct clusters is solid-phase extraction via a pipette tip or spin column, which often leads to loss of low-abundance peptide components. In this study we describe the use of a commercially available surfactant blend that markedly reduces the adduction of monovalent cations during peptide analysis by MALDI-TOFMS.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0951-4198
pubmed:author
pubmed:copyrightInfo
2004 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2953-9
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Removal of sodium and potassium adducts using a matrix additive during matrix-associated laser desorption/ionization time-of-flight mass spectrometric analysis of peptides.
pubmed:affiliation
Invitrogen-Life Technologies Corporation, Carlsbad, CA 92008, USA. john.leite@invitrogen.com
pubmed:publicationType
Journal Article