ON THE CONFORMATIONAL INSTABILITY OF HUMAN SERUM LOW-DENSITY LIPOPROTEIN: EFFECT OF TEMPERATURE*
- A. Scanu†,
- H. Pollard,
- R. Hirz‡, and
- K. Kothary§
- DEPARTMENT OF MEDICINE, CHICAGO
- DEPARTMENT OF BIOCHEMISTRY, UNIVERSITY OF CHICAGO, CHICAGO
- ARGONNE CANCER RESEARCH HOSPITAL, CHICAGO**
Abstract
When examined by circular dichroism and ultraviolet spectroscopy, human serum low-density lipoprotein (LDL) and its delipidated product, apo LDL, exhibited reversible thermal changes. The more marked temperature sensitivity of apo LDL as compared to LDL was taken to support a constraining role by lipids on the observed structural instability of the apoprotein.
Footnotes
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↵ † Recipient of Career Development Award HE-24,867 from the U.S. Public Health Service.
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↵ ‡ U.S. Public Health Service postdoctoral fellow (1-F2-GM33479).
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↵ § Postdoctoral research fellow.
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↵ * This work was supported in part by grants from the U.S. Public Health Service (HE-08727), Life Insurance Medical Research Fund (G68-27), and the Chicago and Illinois Heart Associations (RN68-12).
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↵ ** Operated by the University of Chicago for the U.S. Atomic Energy Commission.
