ArticleProceedings of the National Academy of Sciences of the United States of America1986
Analysis of cDNA clones encoding the entire B-26 region of human apolipoprotein B.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 28 citations in OpenAlex.
- Increased expression of apolipoprotein genes accompanies differentiation in the intestinal cell line Caco-2.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Association between a specific apolipoprotein B mutation and familial defective apolipoprotein B-100.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Two new ApoB gene polymorphisms: Rs1 and Rs2.Nucleic acids research · 1988Article
- Two new ApoB gene polymorphisms: Rs3 and Rs4.Nucleic acids research · 1988Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
We report the characterization of intestine and liver cDNA clones for human apolipoprotein B (apoB) that map to the 5' end of the mRNA. The protein sequence encoded by the 5011 nucleotides derived from sequence analysis of these clones includes 1643 amino acid residues of the mature protein of Mr 184,000. The amino acid sequence at the amino terminus of B-74 peptide was determined and mapped to residue 1298. The size (Mr 145,700) and amino acid composition of the B-26 region encoded by these clones (including amino acid residues 1-1297) closely match the values obtained from the B-26 peptide. The amino acid sequence of peptide B-100 at the junction of peptides B-26 and B-74 (Phe-Lys decreases- Ser) shows structural homology to the site on human kininogen (Phe-Arg decreases- Ser) that is cleaved by the protease plasma kallikrein. The encoded protein contains five potential N-glycosylation sites and several regions in which the hydroxyamino acids, serine and threonine, are present in high abundance. The protein sequence presented in this report represents approximately 30% of the total B-100 protein and will aid in the characterization of additional cDNA clones.
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