Title : Human apolipoprotein A-I forms thermally stable complexes with anionic but not with zwitterionic phospholipids.

Pub. Date : 1986 Dec 5

PMID : 3097001






4 Functional Relationships(s)
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Protein Name
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1 This is again in contrast to apo A-I recombinants with DMPG which show no calorimetrically detectable thermal denaturation, at least in a temperature range up to 100 degrees C. Also circular dichroism data indicate high resistance of apo A-I to thermal unfolding in the presence of DMPG. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens
2 This is again in contrast to apo A-I recombinants with DMPG which show no calorimetrically detectable thermal denaturation, at least in a temperature range up to 100 degrees C. Also circular dichroism data indicate high resistance of apo A-I to thermal unfolding in the presence of DMPG. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens
3 In contrast, complexes of apo A-I with DMPG and other acidic phospholipids may be thermodynamically stable over a wide temperature range greater than or equal to Tc. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens
4 Both apo A-I X DMPC and apo A-I X DMPG complexes form lipoprotein particles having a discoidal shape. dimyristoylphosphatidylglycerol apolipoprotein A1 Homo sapiens