1977
DOI: 10.1111/j.1432-1033.1977.tb11803.x
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Ionization Behaviour of Native Apolipoproteins and of Their Complexes with Lecithin

Abstract: The ionization behaviour of native apoA‐I protein is compared to that of its complex with synthetic dimyristoyl lecithin in studies using calorimetric, potentiometric and spectrophotometric titration. In the presence of phospholipids, 10 out of the 21 lysines together with 22 acidic residues are masked in the complex. All tyrosines remain accessible to titration below pH 13. The apparent ionization enthalpy of the 11 lysine residues is not affected by the presence of phospholipids. These data are consistent wi… Show more

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Cited by 13 publications
(4 citation statements)
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References 27 publications
(22 reference statements)
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“…This means that hydrophobic interactions between the α-helices of lipid free apoA-I might not contribute substantially to the thermodynamic stability of the monomeric state. In conclusion, the thermodynamic properties of lipid free apoA-I at plasma concentrations should be typical for a molten globular state, i.e., the protein has a compact folding, with a core of α-helices bundled via hydrophobic contacts (Barbeau et al, 1979 ; Atkinson and Small, 1986 ; Nolte and Atkinson, 1992 ; Gursky and Atkinson, 1996 ), a reduced cooperative unfolding (Reynolds, 1976 ; Gursky and Atkinson, 1996 ), lacks a defined tertiary structure, has increased solvent access to its hydrophobic surfaces (Reynolds, 1976 ; Rosseneu et al, 1977 ; Gursky and Atkinson, 1996 ), is easily denatured, has high affinity for hydrophobic ligands, and a predisposition to form aggregates (Reynolds, 1976 ; Tall et al, 1976 ).…”
Section: Models Of Lipid Free Apoa-imentioning
confidence: 99%
“…This means that hydrophobic interactions between the α-helices of lipid free apoA-I might not contribute substantially to the thermodynamic stability of the monomeric state. In conclusion, the thermodynamic properties of lipid free apoA-I at plasma concentrations should be typical for a molten globular state, i.e., the protein has a compact folding, with a core of α-helices bundled via hydrophobic contacts (Barbeau et al, 1979 ; Atkinson and Small, 1986 ; Nolte and Atkinson, 1992 ; Gursky and Atkinson, 1996 ), a reduced cooperative unfolding (Reynolds, 1976 ; Gursky and Atkinson, 1996 ), lacks a defined tertiary structure, has increased solvent access to its hydrophobic surfaces (Reynolds, 1976 ; Rosseneu et al, 1977 ; Gursky and Atkinson, 1996 ), is easily denatured, has high affinity for hydrophobic ligands, and a predisposition to form aggregates (Reynolds, 1976 ; Tall et al, 1976 ).…”
Section: Models Of Lipid Free Apoa-imentioning
confidence: 99%
“…For end-point measurements, spectra were recorded between 250 nm and 500 nm, after 4 h incubation of the samples with guanidinium hydrochloride at concentrations varying between 0 M and 7 M. The fluorescence polarization ratiop of the complexes and of the HDL was measured on an Elscint microviscometer [I 71. For kinetic experiments the p value was recorded during 24 h at 25 "C. For the end-point experiments the p value was measured in the temperature range, 15 -4O"C, after 4 h incubation with guanidinium hydrochloride.…”
Section: Incubation With Guanidine Hydrochloridementioning
confidence: 99%
“…The sequences of apoA-1 and other exchangeable apolipoproteins contain characteristic 22-residue tandem repeats (6) predicted to form amphiphatic a-helixes that are proposed to play the key role in the lipid binding (7,8). Long (19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35) amino acids) amphiphatic a-helices packed in elongated bundles have been observed in two apolipoprotein x-ray crystal structures (9,10). CD analysis indicates -85% a-helical content for apoA-1 on HDL, compared to "60% in the lipid-free form (11) that is inferred to have a compact prolate shape (12).…”
mentioning
confidence: 99%