Title : Normalization of receptor binding of apolipoprotein E2. Evidence for modulation of the binding site conformation.

Pub. Date : 1984 Jun 10

PMID : 6327714






4 Functional Relationships(s)
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1 When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding. Dimyristoylphosphatidylcholine apolipoprotein E Homo sapiens
2 When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding. Dimyristoylphosphatidylcholine apolipoprotein E Homo sapiens
3 When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding. Dimyristoylphosphatidylcholine apolipoprotein E Homo sapiens
4 When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding. Dimyristoylphosphatidylcholine apolipoprotein E Homo sapiens