Linked Life Data

10535411

Source:http://linkedlifedata.com/resource/pubmed/id/10535411

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1999-11-16
pubmed:abstractText
The in vitro metabolism of transglutaminase-synthesized substance P analogs has been characterized comparing their stability to that of the parent peptide. The major metabolites have been purified and their structures elucidated by mass spectrometry. Our results demonstrated that gln5 spermidine and spermine analogs of substance P possess an enhanced resistance to the action of proteases. Moreover spermine, a large size hydrophilic compound, specifically prevented the hydrolysis at Phe7-Phe8 bond.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0167-0115
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-80
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Transglutaminase-mediated amine incorporation into substance P protects the peptide against proteolysis in vitro.
pubmed:affiliation
Department of Biochemistry and Biophysics, 2nd University of Naples, Italy. carlaesp@unina.it
pubmed:publicationType
Journal Article