Linked Life Data

6160595

Source:http://linkedlifedata.com/resource/pubmed/id/6160595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1981-2-26
pubmed:abstractText
A series of C-terminal partial sequences of Substance P, either free or blocked at the amino terminus, has been synthesized. The peptides were examined for their relative potencies as smooth muscle contracting agents and for their rates of degradation by rat brain synaptosomes. The C-terminal hexapeptide in both the free and blocked forms displays activity comparable to that of the longer C-terminal peptides as well as to that of the native undecapeptide. The blocked peptides, however, are much more stable than the corresponding free peptides. Among the free peptides Substance P is degraded virtually at the same rate as the C-terminal octapeptide but significantly more slowly than the C-terminal hexa- or heptapeptides. These patterns of inactivation together with the response to inhibition by various protease inhibitors indicate that both endopeptidase(s) are involved in the degradation of Substance P. Degradation of the Substance P molecule at Substance P synapses may occur in two steps, first by a specific endopeptidase splitting the molecule into an N-terminal tetrapeptide and a C-terminal heptapeptide, the latter being degraded in a second step by aminopeptidases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0079-6085
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-94
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Substance P and analogues: biological activity and degradation.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't