Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-7-10
pubmed:abstractText
In a previous study, electrospray ionization mass spectrometry was used to analyze the structure of the O-glycopeptide diptericin, an antibacterial peptide from the fleshfly Phormia terranovae. Several glycoforms of diptericin differing in the length of their oligosaccharide chains were present at the final stage of purification. In order to determine the origin of this glycan heterogeneity, we analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) the relative abundance of the different diptericin glycoforms in fractions obtained after each purification step, and directly in the hemolymph and in the fat body which produces diptericin. MALDI-MS clearly shows that the purification procedure had no effect on the O-linked oligosaccharide chains of diptericin, suggesting that diptericin is synthesized as a family of heterogeneous glycopeptides. In addition, in these experiments, differential mapping by MALDI-MS of the hemolymph and fat body tissue from bacteria-challenged and naive larvae allowed us to detect induced or repressed molecules which may be involved in the immune response of P. terranovae.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
247
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
366-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
A matrix-assisted laser desorption ionization time-of-flight mass spectrometry approach to identify the origin of the glycan heterogeneity of diptericin, an O-glycosylated antibacterial peptide from insects.
pubmed:affiliation
CNRS, Unité Propre de Recherche 9022, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't