Portal de Periódicos da CAPES

Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B.

1986; National Academy of Sciences; Volume: 83; Issue: 5 Linguagem: Inglês

10.1073/pnas.83.5.1467

1091-6490

Andrew A. Protter, D A Hardman, James W. Schilling, Judith Miller, Vanessa L. Appleby, G C Chen, S W Kirsher, Glenn McEnroe, John P. Kane,

Protein Structure and Dynamics

A partial cDNA clone for the B-26 region of apolipoprotein B was isolated from an adult human liver DNA library by screening with an oligonucleotide probe derived from amino-terminal protein sequence obtained from purified B-26 peptide. Antisera against a synthetic 17-residue peptide whose amino acid sequence was encoded by the clone cross-reacts with apolipoproteins B-26, B-100, and B-48, but not with B-74. The nucleotide sequence immediately upstream from the amino terminus of B-26 codes for an apparent signal sequence, implying that the B-26 moiety is in an amino-terminal locus in the B-100 protein. That this sequence represents a 5' end region is further supported by primer extension analysis using a fragment of the cDNA clone and by S1 nuclease protection experiments using the corresponding region in a genomic clone.