The Ca2รท-dependent interaction of various polyanionic polysaccharides (chondroitin sulfate, heparin, dextran sulfate,/~-cyclodextrin sulfate, hyaluronic acid and carboxymethyldextran) with multilamellar dimyristoyl phosphatidylcholine (DMPC) liposomes was investigated by calorimetric and fluorescenc
Adsorption of Milk Proteins to Phosphatidylglycerol and Phosphatidylcholine Liposomes
โ Scribed by Dawn V. Brooksbank; Jeffrey Leaver; David S. Horne
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 305 KB
- Volume
- 161
- Category
- Article
- ISSN
- 0021-9797
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โฆ Synopsis
Interactions between various milk proteins and small unilamellar liposomes at (\mathrm{pH} 6.2) have been followed by measuring the increase in the hydrodynamic radius of the particles using photon correlation spectroscopy. Relatively high salt concentration was required for adsorption of the protein. Observed variations in protein layer thickness between the negatively charged phosphatidylglycerol (PG) liposomes and zwitterionic phosphatidylcholine (PC) liposomes could be explained by reference to the distribution of the charged regions of the proteins and the charge on the surface. Protein layer thicknesses on the negatively charged surface were significantly greater due to charge repulsion between the surface and the negatively charged regions of the proteins. O 1993 Acadcmic Press. Inc.
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