ArticleProceedings of the National Academy of Sciences of the United States of America1985
Molecular cloning and expression of partial cDNAs and deduced amino acid sequence of a carboxyl-terminal fragment of human apolipoprotein B-100.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 57 citations in OpenAlex.
- Genetic variation and atherosclerosis.Current genomics · 2008Article
- 10th International Conference on Methods in Protein Structure Analysis. September 8-13, 1994, Snowbird, Utah. Short communications and abstracts.Journal of protein chemistry · 1994Article
- The apolipoprotein multigene family: structure, expression, evolution, and molecular genetics.Klinische Wochenschrift · 1989Review
- Rapid typing of tandemly repeated hypervariable loci by the polymerase chain reaction: application to the apolipoprotein B 3' hypervariable region.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Rat monoclonal antibodies to rabbit and human serum low-density lipoprotein.The Biochemical journal · 1988Article
- A complex Hind III polymorphism in the human apolipoprotein-B gene (APOB).Nucleic acids research · 1987Article
- The complete sequence and structural analysis of human apolipoprotein B-100: relationship between apoB-100 and apoB-48 forms.The EMBO journal · 1986Article
- Tissue-specific expression and developmental regulation of the rat apolipoprotein B gene.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
- Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
- Determination of the molecular mass of apolipoprotein B-100. A chemical approach.The Biochemical journal · 1986Article
- Analysis of cDNA clones encoding the entire B-26 region of human apolipoprotein B.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
- The isolation of genomic recombinants for the human apolipoprotein B gene and the mapping of three common DNA polymorphisms of the gene--a useful marker for human chromosome 2.Human genetics · 1986Article
- Apolipoprotein B synthesis by human liver and intestine in vitro.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
- Molecular cloning of partial cDNAs for rabbit liver apolipoprotein B and the regulation of its mRNA levels by dietary cholesterol.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
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9 authors at 1 institution in 1 country.
Funding
Abstract
Apolipoprotein (apo) B-100 cDNAs were identified in a human liver cDNA library cloned in the expression vector lambda gt11. The beta-galactosidase-apoB-100 fusion protein was detected by two independently produced low density lipoprotein polyclonal antisera and by three apoB-100 monoclonal antibodies that crossreact with apoB-74. It was not recognized by two apoB-100 monoclonal antibodies that crossreact with apoB-26. The longest clone, lambda B8, was completely sequenced. It contains a 2.8-kilobase DNA fragment containing the codons for the carboxyl-terminal 836 amino acid residues of apo-B-100, as well as the 3' untranslated region of apoB-100 mRNA. We have thus mapped apoB-74 to the carboxyl-terminal portion of apoB-100. The deduced amino acid sequence of the cloned DNA matches the sequences of 14 apoB-100 peptides determined in our laboratory. Minor differences in amino acid sequence were noted in three of the peptides, suggesting polymorphism of apoB-100 at the protein and DNA levels. Secondary structure predictions reveal an unusual pattern for apolipoproteins, consisting of beta-structure (24%), alpha-helical content (33%), and random structure (30%). Ten amphipathic helical regions of 10-24 residues were identified. This carboxyl-terminal fragment of apoB-100 is considerably more hydrophobic than other apolipoproteins with known structure. Its lipid binding regions might include stretches of highly hydrophobic beta-sheets as well as amphipathic helices. Our findings on apoB structure might be important for understanding the role of apoB-100-containing lipoproteins in atherosclerosis.
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