| http://purl.uniprot.org/citations/7918467 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7918467 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7918467 | http://www.w3.org/2000/01/rdf-schema#comment | "We have determined the primary structure of human apolipoprotein D (apoD) by aligning peptides derived from digestions by cyanogen bromide, trypsin, and chymotrypsin. Our results confirm the primary structure derived from cDNA [Drayna et al. (1986) J. Biol. Chem. 261, 16535-16539]. ApoD consists of 169 amino acid residues, including 5 cysteines. Tryptic peptide analysis indicated that Cys41 and Cys16 are joined by a disulfide bridge. Using a combination of manual Edman degradations and mass spectrometric analysis on a purified cluster of chymotryptic fragments, we identified an intramolecular disulfide bridge between Cys8 and Cys114 and an intermolecular bridge between Cys116 of apoD and Cys6 of apoA-II. In addition, sites of N-glycosylation were found at Asn45 and Asn78. Because apoD contains two intramolecular disulfide linkages and has a high content of proline to disrupt alpha-helical structures, formation of the amphipathic helical regions that characterize the other soluble apolipoproteins is unlikely. We conclude that apoD binds to lipoprotein surfaces through structures other than alpha-helices, such as disulfide links."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00207a011"xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00207a011"xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Yang M."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Yang M."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Yang C.-Y."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Yang C.-Y."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Gaskell S.J."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Gaskell S.J."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Gotto A.M. Jr."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Gotto A.M. Jr."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Blanco-Vaca F."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Blanco-Vaca F."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Gu Z.-W."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Gu Z.-W."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Massey J.B."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Massey J.B."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Pownall H.J."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/author | "Pownall H.J."xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/7918467 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |