Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2003-10-2
pubmed:abstractText
We demonstrate the presence in leech hemolymph of high levels of a peptide recognized by antiserum directed against bovine chromacin. The purification of the chromacin-like peptide was carried out by an acidic extraction, followed by solid phase and high pressure gel permeation chromatography and reversed-phase HPLC purification. Its sequence (GDFELPSIADPQATFESQRGPSAQQVDK) was established by a combination of techniques, including automated Edman degradation, MALDI-TOF measurement and DOT immunobinding assays with anti-chromogranin A. Mass spectrometry measurement revealed a m/z 3177Da, revealing the fact that the molecule is phosphorylated. ELISA titrations performed at each step of the purification revealed a major increase in the level of the peptide (ca. 125 nmol/microl of coelomic fluid) 15 min after LPS exposure. The increase in chromacin-like peptide levels is both time and concentration dependent. The level of this peptide decreased significantly 4 hours after LPS exposure. This report is the first discovery of a chromogranin derived like peptide in invertebrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0172-780X
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Chromacin-like peptide in leeches.
pubmed:affiliation
Laboratoire de Neuroimmunologie des Annélides, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq Cedex, France. michel.salzet@univ-lille1.fr
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't