| http://purl.uniprot.org/citations/1554372 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1554372 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1554372 | http://www.w3.org/2000/01/rdf-schema#comment | "Structural and physical properties of glycosylasparaginase (EC 3.5.1.26) from the livers of human, pig, cow, rat, mouse and chicken were compared. The enzyme in all species had a common basic structure of two N-glycosylated subunits of about 24 (alpha) and 20 (beta) kDa joined by non-covalent forces. Subunit-specific antisera against the rat glycosylasparaginase bound specifically and sensitively to the corresponding subunits from all species. Identity of 80% of the amino acids was found between the N-terminal sequences of corresponding pig and rat glycosylasparaginase alpha- and beta-subunits and the deduced sequence from a human glycosylasparaginase cDNA [Fisher, Tollersrud & Aronson (1990) FEBS Lett. 269, 440-444]. The beta-subunit from all three species has an N-terminal threonine reported to be involved in the reaction mechanism for the human enzyme [Kaartinen, Williams, Tomich, Yates, Hood & Mononen (1991) J. Biol. Chem. 266, 5860-5869]. The native enzyme appeared as a heterodimer among the mammals, whereas the chicken enzyme had a greater molecular mass and is probably either a tetramer or a heterodimer bound to an unrelated peptide(s). All glycosylasparaginases were thermostable, requiring temperatures between 65 degrees C and 80 degrees C to be irreversibly inactivated. In addition, they were unusually stable at high pH and remained active in the presence of SDS except at low pH. The pH maximum was between 5.5 and 6 except for the rat and mouse enzymes which had a broad maximum between pH 7 and 8. A number of other properties were observed which also distinguish the enzyme from individual and closely related species."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj2820891"xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj2820891"xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/author | "Aronson N.N. Jr."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/author | "Aronson N.N. Jr."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/author | "Tollersrud O.-K."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/author | "Tollersrud O.-K."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/pages | "891-897"xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/pages | "891-897"xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/title | "Comparison of liver glycosylasparaginases from six vertebrates."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/title | "Comparison of liver glycosylasparaginases from six vertebrates."xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/1554372 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1554372 |
| http://purl.uniprot.org/citations/1554372 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1554372 |
| http://purl.uniprot.org/citations/1554372 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1554372 |
| http://purl.uniprot.org/citations/1554372 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1554372 |
| http://purl.uniprot.org/uniprot/P30919 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1554372 |
| http://purl.uniprot.org/uniprot/P30918 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1554372 |