Linked Life Data

6772203

Source:http://linkedlifedata.com/resource/pubmed/id/6772203

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1980-10-21
pubmed:abstractText
A series of peptides was synthesized with amino acid sequences identical with the cleavage site at which the procollagen N-protease cleaves the N-terminal propeptide from the pro alpha 1 chain of type I procollagen. Peptides up to 11 residues in length did not serve as substrates for the enzyme, an observation consistent with the demonstration that the N-protease will not cleave denatured procollagen or dissociated pro alpha chains. Several of the peptides, however, served as effective inhibitors of the cleavage of procollagen. Comparison of the inhibitor activities of peptides of varying lengths suggested that the L-phenylalanine found three residues to the left of the cleavage site was important for inhibitor activity. This suggestion was confirmed by synthesis of analogues of inhibitory peptides in which L-phenylalanine was replaced by D-phenylalanine, tyrosine, lysine, aspartic acid, or glycine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2646-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Inhibitors of procollagen N-protease. Synthetic peptides with sequences similar to the cleavage site in the pro alpha 1(I) chain.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.