title: Heat denaturation of human high density lipoproteins and chylomicrons.
abstract: 1. The objective of this investigation was to determine whether structural differences between apolipoproteins could be detected by heat denaturation. 2. The apoproteins of human serum high density lipoprotein (HDL2, d = 1.070-1.125 and HDL3, d = 1.125-1.21 g/ml), their major polypeptide constituents (R-Thr and R-Gln), and apochylomicrons were investigated. 3. Heat denaturation was found to be reversible in the temperature range from 20 to 80 degrees. 4. The thermodynamic parameters of heat denaturation delta F, delta H, delta S and delta Cp were calculated on the basis of a single transition from the "native" to "denatured" state for apo-HDL2, apochylomicrons, R-Thr and R-Gln; for apo-HDL3 these parameters were calculated on the basis of two transitions. 5. The thermodynamic parameters, with the exception of delta F, which describe heat denaturation of high density apolipoprotein, of high density apolipoprotein polypeptides and of apochylomicrons were found to be similar on a molar basis and to have approximately the same values as the thermodynamic parameters which describe heat denaturation of non-lipid binding proteins; on a weight basis differences were apparent between the apolipoproteins and the polypeptides or non-lipid binding proteins.
authors.affiliation: Department of Microbiology, University of Southern California School of Medicine, Los Angeles, Calif. 90033, USA.
authors.forename: P
authors.initials: P
authors.lastname: Eggena
authors.forename: F
authors.initials: F
authors.lastname: Aladjem
mesh_terms: D002914:Chylomicrons / Q000097:blood / Q000737:chemistry*; D006358:Hot Temperature; D006801:Humans; D008075:Lipoproteins, HDL / Q000097:blood / Q000737:chemistry*; D011489:Protein Denaturation; D013816:Thermodynamics
chemical_list: D002914:Chylomicrons; D008075:Lipoproteins, HDL