Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-3-27
pubmed:abstractText
The extracellular serylprotease subtilisin Carlsberg (SubC) of Bacillus licheniformis is produced in a precursor form which includes a signal peptide (sp) and a pro-region. We have constructed a fusion protein in which the sp, pro-region and 38 amino acids (aa) at the N terminus of SubC were joined to the immunoglobulin (Ig) G-binding protein G produced by group G streptococci. The fused SubC::protein G was purified on IgG-Sepharose. IgG-binding material derived from membrane or supernatant fractions had different N termini, indicating that release from the membrane occurred only after removal of the pro-region. The proteolytic pattern was identical when SubC::protein G was produced in Bacillus subtilis 168 wild type or in a protease-deficient strain. The sp cleavage point was also defined in the membrane-derived material.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The subtilisin Carlsberg pro-region is a membrane anchorage for two fusion proteins produced in Bacillus subtilis.
pubmed:affiliation
Center for BioTechnology, Karolinska Institute, Huddinge, Sweden.
pubmed:publicationType
Journal Article