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Science 4 October 1985:
Vol. 230. no. 4721, pp. 37 - 43
DOI: 10.1126/science.2994225
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Articles

Science, Vol 230, Issue 4721, 37-43
Copyright © 1985 by American Association for the Advancement of Science

articles

Human apolipoprotein B: structure of carboxyl-terminal domains, sites of gene expression, and chromosomal localization

TJ Knott, SC Rall Jr, TL Innerarity, SF Jacobson, MS Urdea, B Levy-Wilson, LM Powell, RJ Pease, R Eddy, H Nakai, and al. et

Apolipoprotein (apo-) B is the ligand responsible for the receptor-mediated catabolism of low density lipoproteins, the principal cholesterol-transporting lipoproteins in plasma. The primary structure of the carboxyl-terminal 30 percent (1455 amino acids) of human apo-B (apo-B100) has been deduced from the nucleotide sequence of complementary DNA. Portions of the protein structure that may relate to its receptor binding function and lipid binding properties have been identified. The apo-B100 messenger RNA is about 19 kilobases in length. The apo-B100 gene is expressed primarily in liver and, to a lesser extent, in small intestine, but in no other tissues. The gene for apo-B100 is located in the p24 region (near the tip of the short arm) of chromosome 2.


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