Complete cDNA encoding human phospholipid transfer protein from human endothelial cells.
J Biol Chem
; 269(12): 9388-91, 1994 Mar 25.
Article
em En
| MEDLINE
| ID: mdl-8132678
ABSTRACT
Phospholipid transfer protein, with an apparent molecular mass of 81 kDa, was purified from human plasma. The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full-length cDNA from a human endothelial cDNA library. The cDNA is 1,750 base pairs in length and contains an open reading frame of 1,518 nucleotides encoding a leader of 17 amino acids and a mature protein of 476 residues. Northern blot analysis shows a single mRNA transcript of approximately 1.8 kilobases with a wide tissue distribution. The gene was mapped to chromosome 20 using a human/rodent somatic cell hybrid mapping panel. Phospholipid transfer protein was found to be homologous to human cholesteryl ester transfer protein, human lipopolysaccharide-binding protein, and human neutrophil bactericidal permeability increasing protein (20, 24, and 26% identity, respectively).
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Transporte
/
Proteínas de Transferência de Fosfolipídeos
/
Proteínas de Membrana
Limite:
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
1994
Tipo de documento:
Article