Open AccessIsolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B.
Author(s) -
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
Publication year - 1986
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.83.5.1467
Subject(s) - biology , complementary dna , peptide sequence , microbiology and biotechnology , nucleic acid sequence , cdna library , primer (cosmetics) , apolipoprotein b , signal peptide , clone (java method) , primer extension , genetics , biochemistry , dna , nucleotide , gene , chemistry , organic chemistry , cholesterol
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.
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