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Journal of Lipid Research, Vol. 8, 396-405, July 1967
Copyright © 1967 by Lipid Research, Inc.
The Rockefeller University, New York 10021
The antigenicity of ßbeta;-lipoprotein that had been chemically altered by acetylation or arsanilation was compared with that of native ßbeta;-lipoprotein, of lymph chylomicrons, of plasma proteins with d > 1.21, and of plasma from patients with abetalipoproteinemia. Chemical alteration causes structural changes in ßbeta;-lipoprotein which render it immunologically identical with a protein that is present both in normal plasma and in plasma from patients with abetalipoproteinemia. This protein has been identified by immunoelectrophoresis as a ßbeta;-globulin which does not stain for lipid. It is presumed to be the lipid-free apoprotein of ßbeta;-lipoprotein (B protein).
The findings suggest that abetalipoproteinemia is not due to inability to synthesize B protein, but might instead be due to a defect in the formation of the complete ßbeta;-lipoprotein macro-molecule.
Supplementary key words ßbeta;-lipoprotein azo-ßbeta;-lipoprotein acetyl-ßbeta;-lipoprotein antisera B protein plasma 1.21 infranate abetalipoproteinemia lipid transport man
Submitted on March 3, 1967
Accepted on April 20, 1967
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