On the conformational instability of human serum low-density lipoprotein: effect of temperature.
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.
D055598:Chemical Phenomena; D002621:Chemistry; D006801:Humans; D008055:Lipids / Q000032:analysis; D008074:Lipoproteins / Q000097:blood*; D013057:Spectrum Analysis; D013696:Temperature
D008055:Lipids; D008074:Lipoproteins