Title : Mechanism of dissociation of human apolipoprotein A-I from complexes with dimyristoylphosphatidylcholine as studied by guanidine hydrochloride denaturation.

Pub. Date : 1982 Jun 8

PMID : 6809042






4 Functional Relationships(s)
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1 Mechanism of dissociation of human apolipoprotein A-I from complexes with dimyristoylphosphatidylcholine as studied by guanidine hydrochloride denaturation. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
2 In both the denaturation and renaturation of 1:100 and 1:500 complexes, the final values of the molar ellipticity and the ratio of free to bound apo A-I at various concentrations of Gdn-HCl are dependent on the initial state of the lipid and protein; apo A-I is more resistant to denaturation when Gdn-HCl is added to existing complexes than to a mixture of apo A-I and DMPC. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
3 There is an intermediate state in the denaturation pathway of apo A-I/DMPC complexes which is not present in the renaturation; the intermediate comprises partially unfold apo A-I molecules still associated with the complex by some of their apolar residues. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens
4 The energy barrier associated with this desorption step makes the binding of apo A-I to DMPC a thermodynamically irreversible process. Dimyristoylphosphatidylcholine apolipoprotein A1 Homo sapiens