| http://purl.uniprot.org/citations/2644273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2644273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2644273 | http://www.w3.org/2000/01/rdf-schema#comment | "An efficient post-translational assay for solubilized yeast signal peptidase has been developed. The enzyme can be solubilized in nonionic detergent (0.5% Nikkol) without added salt, but salt increased the efficiency of solubilization. Radiosequencing of the cleaved substrate revealed that the enzyme removed the signal peptide. The substrate (prepro-alpha-factor) must be pretreated with sodium dodecyl sulfate to be cleaved. The enzyme displays a broad, alkaline pH optimum, retaining activity at pH 12. Moderately high temperatures (35 degrees C), excess detergent (greater than 0.5% Nikkol), or high salt (greater than 300 mM KOAc) will inactivate the enzyme. Phosphatidylcholine is necessary for optimal activity. The optimal ratio of Nikkol:lipid:sodium dodecyl sulfate is 6.4:2.2:1. The membrane association of yeast signal peptidase is resistant to carbonate extraction, indicating that it is an integral membrane protein."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)81701-5"xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(19)81701-5"xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/author | "Blobel G."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/author | "Blobel G."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/author | "YaDeau J.T."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/author | "YaDeau J.T."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/pages | "2928-2934"xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/pages | "2928-2934"xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/title | "Solubilization and characterization of yeast signal peptidase."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/title | "Solubilization and characterization of yeast signal peptidase."xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/volume | "264"xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://purl.uniprot.org/core/volume | "264"xsd:string |
| http://purl.uniprot.org/citations/2644273 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2644273 |
| http://purl.uniprot.org/citations/2644273 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2644273 |
| http://purl.uniprot.org/citations/2644273 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2644273 |
| http://purl.uniprot.org/citations/2644273 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2644273 |
| http://purl.uniprot.org/uniprot/P15367 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2644273 |
| http://purl.uniprot.org/uniprot/P15367#attribution-CD91A7D0FE9599632224316624C1EF34 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/2644273 |