Linked Life Data

7488030

Source:http://linkedlifedata.com/resource/pubmed/id/7488030

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-11-29
pubmed:abstractText
The primary amino acid sequence of the carboxyl-terminal portion of the alpha 3 chain of chicken type VI collagen (K-VI) presents a 58-residue motif with a high degree of homology with members of the Kunitz serine-proteinase inhibitors family. This module was cloned, expressed in E. coli, purified and compared to the bovine pancreatic trypsin inhibitor (BPTI) in an inhibition profile assay of two serine proteases, trypsin and plasmin. We found that recombinant K-VI is not endowed with inhibitory activity but it slightly activates both plasmin and trypsin, differently from other members of the family. Moreover, the ability to inhibit the serine protease activity is also lacking in the intact type VI collagen molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
215
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1050-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Expression, purification and functional characterisation of a Kunitz-type module from chicken type VI collagen.
pubmed:affiliation
Immunology Section, Department of Sciences and Biomedical Technologies, Udine-Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't