Linked Life Data

3292415

Source:http://linkedlifedata.com/resource/pubmed/id/3292415

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6 Pt 2
pubmed:dateCreated
1988-8-24
pubmed:abstractText
A cell line that secretes substantial quantities of recombinant human prorenin was prepared by transfecting Chinese hamster ovary cells with a gene encoding preprorenin. The prorenin was purified to homogeneity and was found to have a single amino terminus, reflecting cleavage after a typical 23 amino acid signal sequence. The purified inactive prorenin was not a substrate for active renin and was not capable of self-activation. Prorenin could be converted to renin by addition of exogenous protease, and deglycosylation of the prorenin did not alter the sensitivity to protease activation. The enzymatic activity of deglycosylated renin was kinetically identical to that of the native protein. Multimilligram quantities of recombinant human renin and prorenin were purified, providing suitable material for studies directed toward greater understanding of the function of these proteins and for structural studies such as x-ray diffraction for use in design of renin inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0194-911X
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
713-6
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Characterization of recombinant human prorenin and renin.
pubmed:affiliation
California Biotechnology, Inc., Mountain View 94043.
pubmed:publicationType
Journal Article