| http://purl.uniprot.org/citations/6489332 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/6489332 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/6489332 | http://www.w3.org/2000/01/rdf-schema#comment | "Apolipoprotein A-IGiessen is a variant form of apo A-I that is displaced from the corresponding normal A-I isoforms on isoelectric focusing gels by a single charge unit towards the cathode [Utermann et al. (1982) J. Biol. Chem. 257, 501-507]. Three subjects heterozygous for the variant were detected in one family. The percentage of the total A-I in plasma represented by the A-IGiessen in these subjects ranged over 25-30%. The variant and normal major A-I isoforms from the proband (Y.J.) were purified by preparative isoelectric focusing and cleaved with CNBr. Analytical focusing of CNBr fragments demonstrated a charge difference between CB3Giessen and normal CB3. Sequence analysis of CB3Giessen revealed that a proline existing in normal A-I was replaced by an arginine in the variant A-I at residue 143. The ability of the mutant A-I to activate purified lecithin:cholesterol acyltransferase was determined in vitro. The cofactor activity of [Arg143]apolipoprotein A-I was about 60-70% of that demonstrated by control A-I. Residue 143 is in a putative beta-turn between two of the repeating amphiphilic helices in apolipoprotein A-I and may be a critical determinant of the protein's structure and function."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1984.tb08467.x"xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1984.tb08467.x"xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Steinmetz A."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Steinmetz A."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Haas J."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Haas J."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Paetzold R."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Paetzold R."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Mahley R.W."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Mahley R.W."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Rall S.C. Jr."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Rall S.C. Jr."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Utermann G."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Utermann G."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Weisgraber K.H."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/author | "Weisgraber K.H."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/date | "1984"xsd:gYear |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/date | "1984"xsd:gYear |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/pages | "325-331"xsd:string |
| http://purl.uniprot.org/citations/6489332 | http://purl.uniprot.org/core/pages | "325-331"xsd:string |