| http://purl.uniprot.org/citations/9359845 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9359845 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9359845 | http://www.w3.org/2000/01/rdf-schema#comment | "Human lactoferrin (hLF), a protein involved in host defence against infection and excessive inflammation, interacts with heparin, the lipid A moiety of bacterial lipopolysaccharide, human lysozyme (hLZ) and DNA. To determine which region of the molecule is important in these interactions, solid-phase ligand binding assays were performed with hLF from human milk (natural hLF) and N-terminally deleted hLF variants. Iron-saturated and natural hLF bound equally well to heparin, lipid A, hLZ and DNA. Natural hLF lacking the first two N-terminal amino acids (Gly1-Arg2) showed reactivities of one-half, two-thirds, one-third and one-third towards heparin, lipid A, hLZ and DNA respectively compared with N-terminally intact hLF. A lack of the first three residues (Gly1-Arg2-Arg3) decreased binding to the same ligands to one-eighth, one-quarter, one-twentieth and one-seventeenth respectively. No binding occurred with a mutant lacking the first five residues (Gly1-Arg2-Arg3-Arg4-Arg5). An anti-hLF monoclonal antibody (E11) that reacts to an N-lobe epitope including Arg5 completely blocked hLF-ligand interaction. These results show that the N-terminal stretch of four consecutive arginine residues, Arg2-Arg3-Arg4-Arg5, has a decisive role in the interaction of hLF with heparin, lipid A, hLZ and DNA. The role of limited N-terminal proteolysis of hLF in its anti-infective and anti-inflammatory properties is discussed."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3280145"xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3280145"xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "Nuijens J.H."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "Nuijens J.H."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "de Boer H.A."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "de Boer H.A."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "Mericskay M."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "Mericskay M."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "Geerts M.E."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "Geerts M.E."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "van Berkel P.H."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "van Berkel P.H."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "van Veen H.A."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/author | "van Veen H.A."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/pages | "145-151"xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/pages | "145-151"xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/title | "N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA."xsd:string |
| http://purl.uniprot.org/citations/9359845 | http://purl.uniprot.org/core/title | "N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA."xsd:string |