Linked Life Data

3555496

Source:http://linkedlifedata.com/resource/pubmed/id/3555496

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-6-11
pubmed:abstractText
Paired basic residues are known as a typical site for proteolytic processing of precursors of bioactive peptides. By using a fluorogenic substrate Boc-Gln-Arg-Arg-MCA, a unique endoprotease exhibiting hydrolytic specificity toward the carboxyl side of paired basic residues was partially purified (about 4600-fold) from the membrane fraction of yeast Saccharomyces cerevisiae alpha-cells. The enzyme is a calcium-dependent thiol protease, with optimal pH at 7.0. It is a glycoprotein, with an apparent molecular weight of about 100,000-120,000. It cleaves fluorogenic substrates and a synthetic model peptide at the carboxyl side of paired basic residues. From its unique substrate specificity, this enzyme may be involved in precursor processing in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
807-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
A membrane-bound, calcium-dependent protease in yeast alpha-cell cleaving on the carboxyl side of paired basic residues.
pubmed:publicationType
Journal Article