Structural comparison of human apolipoproteins B-48 and B-100

In this study we have investigated the structural relationship between human apolipoproteins B-48 and B-100 by comparing protein structure and by comparing nucleotide sequence from intestinal and hepatic cDNA clones. Sequences from intestinal and hepatic cDNA were identical over the entire distance...

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Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 26; no. 17; pp. 5478 - 5486
Main Authors:	Hardman, David A, Protter, Andrew A, Chen, G. Chi, Schilling, James W, Sato, Kevin Y, Lau, Kenneth, Yamanaka, Miles, Mikita, Teri, Miller, Judith
Format:	Journal Article
Language:	English
Published:	Washington, DC American Chemical Society 25-08-1987
Subjects:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Apolipoprotein B-100 Apolipoprotein B-48 Apolipoproteins B - genetics Base Sequence Biological and medical sciences Cloning, Molecular DNA - metabolism Fundamental and applied biological sciences. Psychology Humans Immune Sera Intestinal Mucosa - metabolism Lipoproteins, myelin Liver - metabolism Molecular Sequence Data Peptide Fragments - isolation & purification Proteins Human Molecular form Complementary DNA Liver Gut Homology Apolipoproteins
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Summary:	In this study we have investigated the structural relationship between human apolipoproteins B-48 and B-100 by comparing protein structure and by comparing nucleotide sequence from intestinal and hepatic cDNA clones. Sequences from intestinal and hepatic cDNA were identical over the entire distance analyzed (7194 bases), which is more than required to code for B-48. The amino-terminal amino acid sequences from intact B-48 and B-100 proteins were also identical over the entire distance analyzed (16 residues). Additional protein homology was evaluated by the combined techniques of peptide mapping and immunoblotting. Purified B-48 and B-100 were each digested with three different endoproteases, and the resulting peptides were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Peptide bands were then detected by silver stain and by Western blotting with antisera against specific regions of B-48 and B-100. The resulting patterns suggest that B-48 is extensively homologous with the amino-terminal portion of B-100. We have identified only four peptides from B-48 (at least one in each digest) that are absent from the parallel digests of B-100. These peptides appear to arise from the ultimate carboxyl terminus of B-48 and appear to be totally homologous with a region located near the center of B-100. Our observations suggest that mature, circulating B-48 is homologous over its entire length (estimated to be between 2130 and 2144 amino acid residues) with the amino-terminal portion of B-100 and contains no sequence from the carboxyl end of B-100.
Bibliography:	ark:/67375/TPS-C1LNVHWN-P istex:D2A5D4070F954B8E716B7571B9BF9546806B8980 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi00391a040