| http://purl.uniprot.org/citations/3142486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3142486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3142486 | http://www.w3.org/2000/01/rdf-schema#comment | "Extracellular RNase Fl1 has been purified from the culture filtrate of Fusarium lateritium. The enzyme has been obtained in the electrophoretically homogeneous state with the yield about 90% and 300 fdd degree of purification. RNase Fl1 is a guanyl specific enzyme (EC 3.1.27.3) with the specific activity on RNA 1420 units/mg of protein. The total primary structure of the RNase has been determined by the automated Edman degradation of two non-fractionated peptide hydrolysates produced by trypsin and Staphylococcus aureus protease and of the hydroxylamine cleavage products of the protein. It was shown that hydroxylamine converts the RNase Fl1 N-terminal residue, pyroglutamic acid, into the hydroxyamic acid derivative sensitive to Edman degradation. RNase Fl1 consists of 105 amino acid residues (Mr 10,852) and is a structural homologue of the Fus. moniliforme RNase F1, differing from the latter by 15 amino acid substitutions outside the enzyme active site."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/author | "Shlyapnikov S.V."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/author | "Shlyapnikov S.V."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/author | "Bezborodova S.I."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/author | "Bezborodova S.I."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/author | "Chepurnova N.K."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/author | "Chepurnova N.K."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/name | "Bioorg. Khim."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/name | "Bioorg. Khim."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/pages | "893-904"xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/pages | "893-904"xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/title | "Ribonuclease Fl1 from Fusarium lateriticum. Isolation, substrate specificity and amino acid sequence."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/title | "Ribonuclease Fl1 from Fusarium lateriticum. Isolation, substrate specificity and amino acid sequence."xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/3142486 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3142486 |
| http://purl.uniprot.org/citations/3142486 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3142486 |
| http://purl.uniprot.org/citations/3142486 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3142486 |
| http://purl.uniprot.org/citations/3142486 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3142486 |
| http://purl.uniprot.org/uniprot/P16411 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3142486 |
| http://purl.uniprot.org/uniprot/#_P16411-citation-3142486 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/3142486 |