Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-2-7
pubmed:abstractText
A serine protease which catalyses the conversion of the precursor of ANF (atrial natriuretic factor) to the active circulating form, ANF-(99-126)-octacosapeptide, was purified from a particulate fraction of bovine atria. The enzyme was solubilized with a buffer containing 1.6M KCl. The molecular mass of the purified enzyme was 580 kDa on gel filtration, whereas on sodium dodecyl sulfate-polyacrylamide gel electrophoresis a cluster of six bands with molecular masses around 30 kDa was observed. The purified enzyme produced the ANF-(99-126)-octacosapeptide from partially purified bovine pro-ANF by the selective cleavage of the arginyl peptide bond in the -Pro97-Arg98-Ser99-sequence in pro-ANF. It is likely that the enzyme selectively cleaves the Arg98-Ser99 peptide bond in pro-ANF when ANF is secreted into the circulation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
369 Suppl
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-20
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification of a specific peptidase in bovine atria for the processing of pro-atrial natriuretic factor.
pubmed:affiliation
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.