Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1980 May;77(5):2465–2469. doi: 10.1073/pnas.77.5.2465

Heterogeneity of apolipoprotein B: isolation of a new species from human chylomicrons.

J P Kane, D A Hardman, H E Paulus
PMCID: PMC349420  PMID: 6930644

Abstract

Low density lipoproteins and the triglyceride-rich lipoproteins of human serum each contain proteins of high molecular weight termed apolipoprotein B, which have previously been thought to be identical. We have isolated four species of apolipoprotein B with unique molecular weights and amino acid compositions. We have assigned numerical designations to these species in a centile system based upon their relative apparent Mr in NaDodSO4. One which we term B-100, with an apparent Mr of 549,000 +/- 7650 (SD) determined by NaDodSO4 gel electrophoresis, predominates in low density and very low density lipoproteins and is also present in chylomicrons from thoracic duct lymph or from plasma. Substantial amounts of two large proteins designated B-74 (apparent Mr 407,000 +/- 5790) and B-26 (apparent Mr 144,500 +/- 8970), which appear to be complementary fragments or constituents of the B-100 protein, are found in the low density lipoproteins of many individuals. A distinct protein, B-48, with an apparent Mr of 264,000 +/- 8150 is a major and constant constituent of chylomicrons from thoracic duct lymph or from plasma.

Full text

PDF
2465

Images in this article

2466Image
on p.2466

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bilheimer D. W., Eisenberg S., Levy R. I. The metabolism of very low density lipoprotein proteins. I. Preliminary in vitro and in vivo observations. Biochim Biophys Acta. 1972 Feb 21;260(2):212–221. doi: 10.1016/0005-2760(72)90034-3. [DOI] [PubMed] [Google Scholar]
  2. Chapman M. J., Kane J. P. Stability of the apoprotein of human serum low density lipoprotein: absence of endogenous endopeptidase activity. Biochem Biophys Res Commun. 1975 Oct 6;66(3):1030–1036. doi: 10.1016/0006-291x(75)90743-3. [DOI] [PubMed] [Google Scholar]
  3. Chen C. H., Aladjem F. Further studies on the subunit structure of human serum low density lipoproteins. Biochem Med. 1978 Apr;19(2):178–187. doi: 10.1016/0006-2944(78)90019-4. [DOI] [PubMed] [Google Scholar]
  4. HAVEL R. J., EDER H. A., BRAGDON J. H. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J Clin Invest. 1955 Sep;34(9):1345–1353. doi: 10.1172/JCI103182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Innerarity T. L., Mahley R. W. Enhanced binding by cultured human fibroblasts of apo-E-containing lipoproteins as compared with low density lipoproteins. Biochemistry. 1978 Apr 18;17(8):1440–1447. doi: 10.1021/bi00601a013. [DOI] [PubMed] [Google Scholar]
  6. Kane J. P., Richards E. G., Havel R. J. Subunit heterogeneity in human serum beta lipoprotein. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1075–1082. doi: 10.1073/pnas.66.4.1075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kane J. P., Sata T., Hamilton R. L., Havel R. J. Apoprotein composition of very low density lipoproteins of human serum. J Clin Invest. 1975 Dec;56(6):1622–1634. doi: 10.1172/JCI108245. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Morrisett J. D., Jackson R. L., Gotto A. M., Jr Lipoproteins: structure and function. Annu Rev Biochem. 1975;44:183–207. doi: 10.1146/annurev.bi.44.070175.001151. [DOI] [PubMed] [Google Scholar]
  9. Noble R. P. Electrophoretic separation of plasma lipoproteins in agarose gel. J Lipid Res. 1968 Nov;9(6):693–700. [PubMed] [Google Scholar]
  10. Pollard H., Scanu A. M., Taylor E. W. On the geometrical arrangement of the protein subunits of human serum low-density lipoprotein: evidence for a dodecahedral model. Proc Natl Acad Sci U S A. 1969 Sep;64(1):304–310. doi: 10.1073/pnas.64.1.304. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Sigurdsson G., Nicoll A., Lewis B. Conversion of very low density lipoprotein to low density lipoprotein. A metabolic study of apolipoprotein B kinetics in human subjects. J Clin Invest. 1975 Dec;56(6):1481–1490. doi: 10.1172/JCI108229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Socorro L., Camejo G. Preparation and properties of soluble, immunoreactive apoLDL. J Lipid Res. 1979 Jul;20(5):631–638. [PubMed] [Google Scholar]
  13. Steele J. C., Jr, Reynolds J. A. Characterization of the apolipoprotein B polypeptide of human plasma low density lipoprotein in detergent and denaturation solutions. J Biol Chem. 1979 Mar 10;254(5):1633–1638. [PubMed] [Google Scholar]
  14. Steele J. C., Jr, Reynolds J. A. Molecular weight and hydrodynamic properties of apolipoprotein B in guanidine hydrochloride and sodium dodecyl sulfate solutions. J Biol Chem. 1979 Mar 10;254(5):1639–1643. [PubMed] [Google Scholar]
  15. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES