Advertisement

Research Article Free access | 10.1172/JCI106945

Evidence for the identity of the major apoprotein in low density and very low density lipoproteins in normal subjects and patients with familial hyperlipoproteinemia

A. M. Gotto, W. V. Brown, R. I. Levy, Maria E. Birnbaumer, and D. S. Fredrickson

1Molecular Disease Branch, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014

Find articles by Gotto, A. in: PubMed | Google Scholar

1Molecular Disease Branch, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014

Find articles by Brown, W. in: PubMed | Google Scholar

1Molecular Disease Branch, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014

Find articles by Levy, R. in: PubMed | Google Scholar

1Molecular Disease Branch, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014

Find articles by Birnbaumer, M. in: PubMed | Google Scholar

1Molecular Disease Branch, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014

Find articles by Fredrickson, D. in: PubMed | Google Scholar

Published June 1, 1972 - More info

Published in Volume 51, Issue 6 on June 1, 1972
J Clin Invest. 1972;51(6):1486–1494. https://doi.org/10.1172/JCI106945.
© 1972 The American Society for Clinical Investigation
Published June 1, 1972 - Version history
View PDF
Abstract

The major apoprotein(s) from human plasma low density lipoproteins was isolated and compared with a major protein fraction (fraction I) from very low density lipoproteins (VLDL). Fraction I had been previously found to comprise approximately 40% of the total protein of VLDL. Fraction I from VLDL and apoLDL from normal subjects were indistinguishable in amino acid compositions and circular dichroic spectra. They yielded indistinguishable displacement curves of LDL-125I by radioimmunoassay and formed immunoprecipitin lines of complete identity. Fraction I from VLDL of normal subjects was compared with the fraction isolated from patients with familial types II, III, IV, and V hyperlipoproteinemia. There were no detectable differences between any of these fractions in amino acid compositions, circular dichroic spectra, and immunochemical properties. It was, therefore, concluded that short of peptide mapping or determination of amino acid sequence, fraction I from VLDL of each subject with familial hyperlipoproteinemia appears to be identical with fraction I and apoLDL from normal individuals.

A new convenient method of preparation of soluble apoLDL, modified from a procedure previously described from this laboratory, is presented.

Images.

Browse pages

Click on an image below to see the page. View PDF of the complete article

Version history
  • Version 1 (June 1, 1972): No description
Advertisement
Advertisement