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Cited by 279

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Purification of the low density lipoprotein receptor, an acidic glycoprotein of 164,000 molecular weight.

Schneider, W J, Beisiegel, U, Goldstein, J L, Brown, M S·1982·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)34975-5
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Abstract

This paper describes a rapid two-step procedure for the purification of the low density lipoprotein receptor from bovine adrenal cortex membranes. After solubilization with nonionic detergents, the receptor adheres tightly to a DEAE-cellulose column at pH 6. Following elution from DEAE-cellulose, detergent is removed, leaving the receptor in a soluble form. The receptor is then subjected to affinity chromatography on low density lipoprotein coupled to Sepharose 4B. The receptor is eluted with suramin, a newly-found inhibitor of low density lipoprotein-receptor interactions. This procedure yields a single protein with a molecular weight of 164,000. The same protein is also isolated when the crude DEAE-cellulose fraction is applied to an immunoaffinity column containing a monoclonal antibody directed against the receptor. The 164,000-dalton receptor protein has an acidic isoelectric point of 4.6, which rises to 4.8 after extensive treatment with neuraminidase. The purified receptor retains all of the binding properties of the receptor of intact cells and crude membranes.

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Crossref · 10.1016/s0021-9258(18)34975-5

Cites

1 of 1 references verified0 citation errors · 0 not checkable

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Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • LDLRs were originally purified from cow adrenal glands because they were the richest source.

    “Indeed, LDLRs were originally purified from cow adrenal glands because they were the richest source (34, 35).”

    From Last step in the path of LDL cholesterol from lysosome to plasma membrane to ER is governed by phosphatidylserine (2020) · cites this paper as [35]

  • The LDLR peptide has an N-terminal ligand binding domain with high affinity for Apolipoprotein E and Apolipoprotein B, the main structural components of VLDL/LDL.

    “The LDLR peptide has an N-terminal ligand binding domain which has high affinity for Apolipoprotein E74,75, as well as Apolipoprotein B (ApoB)76, the main structural components of VLDL/LDL.”

    From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [76]

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 21

  1. Goldstein, 1977, Annu. Rev. Biochem., 46, 897, 10.1146/annurev.bi.46.070177.004341 · DOI · Paper page
  2. Brown, 1979, Recent Prog. Hormone Res., 35, 215
  3. Schneider, 1979, Proc. Natl. Acad. Sci. U. S. A., 76, 5577, 10.1073/pnas.76.11.5577 · DOI
  4. Schneider, 1980, J. Biol. Chem., 255, 11442, 10.1016/S0021-9258(19)70311-1 · DOI
  5. Weisgraber, 1978, J. Biol. Chem., 253, 9053, 10.1016/S0021-9258(17)34284-9 · DOI
  6. Pitas, 1979, Proc. Natl. Acad. Sci. U. S. A., 76, 2311, 10.1073/pnas.76.5.2311 · DOI · Paper page
  7. Beisiegel, 1981, J. Biol. Chem., 256, 11923, 10.1016/S0021-9258(19)68494-2 · DOI · Paper page
  8. Pharmacia Fine Chemicals (1979) Affinity Chromatography. Uppsala, Sweden, pp. 15–18
  9. Scatchard, 1949, Ann. N. Y. Acad. Sci., 51, 660, 10.1111/j.1749-6632.1949.tb27297.x · DOI
  10. Brown, 1974, Proc. Natl. Acad. Sci. U. S. A., 71, 788, 10.1073/pnas.71.3.788 · DOI
  11. Fraker, 1978, Biochem. Biophys. Res. Commun., 80, 849, 10.1016/0006-291X(78)91322-0 · DOI
  12. Laemmli, 1970, Nature (Lond.), 227, 680, 10.1038/227680a0 · DOI · Paper page
  13. O'Farrell, 1975, J. Biol. Chem., 250, 4007, 10.1016/S0021-9258(19)41496-8 · DOI
  14. Merril, 1981, Science, 211, 1437, 10.1126/science.6162199 · DOI
  15. Swanstrom, 1978, Anal. Biochem., 86, 184, 10.1016/0003-2697(78)90333-0 · DOI
  16. Lowry, 1951, J. Biol. Chem., 193, 265, 10.1016/S0021-9258(19)52451-6 · DOI
  17. Brown, 1981, Science, 212, 628, 10.1126/science.6261329 · DOI · Paper page
  18. Simons, 1978, Proc. Natl. Acad. Sci. U. S. A., 75, 5306, 10.1073/pnas.75.11.5306 · DOI
  19. Brown, 1978, J. Supramol. Struct., 8, 223, 10.1002/jss.400080302 · DOI
  20. Basu, 1976, Proc. Natl. Acad. Sci. U. S. A., 73, 3178, 10.1073/pnas.73.9.3178 · DOI
  21. Mahley, 1977, J. Biol. Chem., 252, 7279, 10.1016/S0021-9258(19)66966-8 · DOI

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Metadata

Authors
Schneider, W. J., Beisiegel, U., Goldstein, J. L., & Brown, M. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1982-03
Volume
257
Issue
5
Pages
2664-2673
ISSN
0021-9258
DOI
10.1016/s0021-9258(18)34975-5
Cited by
279
References
1
Language
en
Licence

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