Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B.
Article Details
- CitationCopy to clipboard
Protter AA, Hardman DA, Schilling JW, Miller J, Appleby V, Chen GC, Kirsher SW, McEnroe G, Kane JP
Isolation of a cDNA clone encoding the amino-terminal region of human apolipoprotein B.
Proc Natl Acad Sci U S A. 1986 Mar;83(5):1467-71.
- PubMed ID
- 3513177 [ View in PubMed]
- Abstract
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.