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Literature DB >> 2811608

Effect of phosphatidylcholine on the alpha-lactalbumin-induced fusion of vesicles.

Abstract

Previous studies on alpha-lactalbumin induced fusion of phosphatidylserine/phosphatidylethanolamine vesicles are extended to vesicles composed of various combinations of phosphatidylserine, phosphatidylethanolamine, phosphatidylcholine and cardiolipin. It was found that inclusion of phosphatidylcholine in the vesicles results in a depression of fusion. This depression of fusion appears to be caused by a reduction in the amount of irreversibly bound alpha-lactalbumin to vesicles containing phosphatidylcholine. It is suggested that in this system fusion is dependent upon the extent by which a particular protein segment penetrates the bilayer.

Entities: Chemical Disease Gene

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Year: 1989 PMID： 2811608 DOI： 10.1007/bf02535759

Source DB: PubMed Journal: Lipids ISSN： 0024-4201 Impact factor: 1.880

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References

13 in total

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Authors: J Kim; H Kim
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Authors: A Portis; C Newton; W Pangborn; D Papahadjopoulos
Journal: Biochemistry Date: 1979-03-06 Impact factor: 3.162

Effect of phosphatidylcholine on the alpha-lactalbumin-induced fusion of vesicles.

1. Studies on membrane fusion. III. The role of calcium-induced phase changes.

2. Large volume liposomes by an ether vaporization method.

3. Interaction of alpha-lactalbumin with phospholipid vesicles as studied by photoactivated hydrophobic labeling.

4. Trypsin action on the growth of Sendai virus in tissue culture cells. 3. Structural difference of Sendai viruses grown in eggs and tissue culture cells.

5. Membrane fusion and molecular segregation in phospholipid vesicles.

6. Tetanus toxin is labeled with photoactivatable phospholipids at low pH.

Review 7. Do hydrophobic sequences cleaved from cellular polypeptides induce membrane fusion reactions in vivo?

8. A universal reagent for phospholipid analysis.

9. Fusion of phospholipid vesicles induced by alpha-lactalbumin at acidic pH.

10. Studies on the mechanism of membrane fusion: evidence for an intermembrane Ca2+-phospholipid complex, synergism with Mg2+, and inhibition by spectrin.