The molecular behavior of apoA-I in human high density lipoproteins.
The properties of apoA-I in human high density lipoprotein (1.063 smaller than d smaller than 1.210 gm per ml) have been examined by fluorescence and difference absorption spectroscopy, while the behavior of the total complement of apoproteins has been evaluated by far ultraviolet circular dichroism. Marked increases in stability to temperature, pH, and guanidine hydrochloride were observed for apoA-I in the native particle as compared to the isolated state.
D001059:Apoproteins; D006146:Guanidines; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008075:Lipoproteins, HDL; D008297:Male; D011487:Protein Conformation; D011489:Protein Denaturation; D013053:Spectrophotometry; D013696:Temperature; D014364:Tryptophan
D001059:Apoproteins; D006146:Guanidines; D008075:Lipoproteins, HDL; D014364:Tryptophan