The effects of proteins on divalent cation-induced phospholipid vesicle aggregation and phospholipid vesicle-monolayer membrane interactions (fusion) were examined. Glycophorin (from human erythrocytes) suppressed the membrane interactions more than N-2 protein (from human brain myelin) when these p
Inhibition effect of aggregation of phospholipid vesicles by incorporation of glycolipids
โ Scribed by Shinji Takeoka; Hiromi Sakai; Hiroyuki Ohno; Kiyoshi Yoshimura; Eishun Tsuchida
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 563 KB
- Volume
- 152
- Category
- Article
- ISSN
- 0021-9797
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๐ SIMILAR VOLUMES
Large unilamellar vesicles composed of a nonionic synthetic glycolipid, 1,3-di-O-phytanyl-2-O-(beta-D-maltotriosyl)glycerol exhibited a pH-dependent aggregation-disaggregation process; vesicle aggregation occurred in a lower pH region and vesicle disaggregation occurred in a higher pH region. This p
Cation-induced aggregation of acidic phospholipid vesicles consisting of dimyristoylphosphatidylglycerol (DMPG), dipalmitoylphosphatidylserine (DPPS), phosphatidylserine from bovine brain (brPS), and phosphatidylglycerol from egg yolk (eggPG) was studied. Significant differences were evident in the