Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1991-12-2
pubmed:abstractText
Galanin is present in high concentrations in porcine adrenals, but nothing is known about the processing and secretion of other products of the 123-amino acid precursor preprogalanin. Using, in combination, RIA against galanin, a variety of chromatographic procedures, mass spectrometry, and amino acid sequencing, we studied the processed and the secreted products of preprogalanin. From the tissue extracts we isolated in equimolar amounts and sequenced two major pools of galanin immunoreactive peptides: galanin and two N-terminally extended forms, preprogalanin-(24-61) and preprogalanin-(26-61). The same peptides were identified upon gel chromatography and analytical HPLC in effluents collected during electrical stimulation of the intact splanchnic nerve supply of an isolated perfused preparation of porcine adrenals. The processing of preprogalanin in porcine adrenals thus includes the formation and release of galanin, preprogalanin-(24-61), and preprogalanin-(26-61). The signal peptidase cleaves the preprogalanin at either Gly23 or Gly25.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2693-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Galanin and galanin extended at the N-terminus with seven and nine amino acids are produced in and secreted from the porcine adrenal medulla in almost equal amounts.
pubmed:affiliation
Department of Medical Physiology C, Panum Institute, University of Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't