The primary structure of human apolipoprotein A-IV.
Biochim Biophys Acta
; 1002(2): 231-7, 1989 Apr 03.
Article
em En
| MEDLINE
| ID: mdl-2930771
ABSTRACT
Human apolipoprotein (apo) A-IV was purified from chylous ascites fluid. Proteolytic peptides produced by trypsin and Staphylococcus aureus V8 proteinase digestions were purified by high-performance liquid chromatography and sequenced. Human apoA-IV contains 376 amino acid residues. The peptide-derived sequence generally matches two previously reported DNA-derived amino acid sequences except for discrepancies in five positions. In order to examine these discrepancies further, one complete apoA-IV cDNA clone and another partial clone were sequenced. Comparison of all the available information indicates that the peptide-derived sequence reported here is accurate. Sequencing errors probably account for some of the discrepancies between the two primary sequences predicted by earlier nucleotide analyses. In certain positions, however, bona fide sequence heterogeneity or cloning artifact cannot be excluded.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Apolipoproteínas A
Limite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1989
Tipo de documento:
Article