Isolation of a cDNA Clone Encoding the Amino-Terminal Region of Human Apolipoprotein B

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 aci...

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Veröffentlicht in:Proc. Natl. Acad. Sci. U.S.A.; (United States) 1986-03, Vol.83 (5), p.1467-1471
Hauptverfasser: Protter, Andrew A., Hardman, David A., Schilling, James W., Miller, Judith, Appleby, Vanessa, Chen, Geri C., Kirsher, Steven W., McEnroe, Glenn, Kane, John P.
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Sprache:eng
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Zusammenfassung: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.83.5.1467