| http://purl.uniprot.org/citations/3732265 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3732265 | http://www.w3.org/2000/01/rdf-schema#comment | "We have purified secreted acid phosphatase of Schizosaccharomyces pombe. The enzyme is N-glycosylated, the associated carbohydrate accounts for 90% of the total molecular mass and the protein moiety has a molecular mass of 54 kDa. The deglycosylated enzyme still exhibits enzymatic activity. Using antibodies recognizing the protein moiety of the enzyme we have identified two intracellular precursors of acid phosphatase: an unglycosylated membrane-bound 54-kDa form that accumulates in the presence of tunicamycin and a partially glycosylated 72-kDa form that accumulates mostly in membranes of cells grown in rich medium. We further showed that the conversion of the 54-kDa and 72-kDa forms to partially glycosylated and fully glycosylated acid phosphatase is a regulated process. Growth conditions determine how much of translated 54-kDa acid phosphatase is glycosylated to the 72-kDa form and how much remains unglycosylated in membranes. When cells are grown in a rich medium, 5% of the total acid phosphatase protein remains as unglycosylated enzyme and 8% as partially glycosylated 72-kDa form. In cells grown in the minimal medium, however, all of the 54-kDa and 72-kDa forms of acid phosphatase are rapidly processed to fully glycosylated enzyme. The 72-kDa form and the unglycosylated form of acid phosphatase are not secreted or transported to the plasma membrane."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1986.tb09730.x"xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/author | "Trachsel H."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/author | "Schweingruber M.E."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/author | "Schweingruber A.M."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/author | "Keller L."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/author | "Schwaninger R."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/author | "Schoenholzer F."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/pages | "133-140"xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/title | "Glycosylation and secretion of acid phosphatase in Schizosaccharomyces pombe."xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://purl.uniprot.org/core/volume | "158"xsd:string |
| http://purl.uniprot.org/citations/3732265 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3732265 |
| http://purl.uniprot.org/citations/3732265 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3732265 |
| http://purl.uniprot.org/uniprot/P08091#attribution-D956EB9CDE5E78B0CC18A80FC021665F | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/3732265 |
| http://purl.uniprot.org/uniprot/#_P08091-mappedCitation-3732265 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/3732265 |
| http://purl.uniprot.org/uniprot/P08091 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/3732265 |