Lysozyme interaction with liposomes: thermodynamics of binding
Using the method of competitive analysis the interaction of lysozyme with liposomes composed of phosphatidyicholine and diphosphatidylglycerot has been studied. In terms of the lattice and continuum models of large ligand adsorption to membrane thermodynamic parameters for the protein-lipid complexe...
Збережено в:
| Дата: | 1999 |
|---|---|
| Автор: | |
| Формат: | Стаття |
| Мова: | English |
| Опубліковано: |
Інститут молекулярної біології і генетики НАН України
1999
|
| Назва видання: | Биополимеры и клетка |
| Теми: | |
| Онлайн доступ: | http://dspace.nbuv.gov.ua/handle/123456789/156821 |
| Теги: |
Додати тег
Немає тегів, Будьте першим, хто поставить тег для цього запису!
|
| Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Цитувати: | Lysozyme interaction with liposomes: thermodynamics of binding / G.P. Gorbenko // Биополимеры и клетка. — 1999. — Т. 15, № 6. — С. 481-486. — Бібліогр.: 19 назв. — англ. |
Репозитарії
Digital Library of Periodicals of National Academy of Sciences of Ukraine| Резюме: | Using the method of competitive analysis the interaction of lysozyme with liposomes composed of phosphatidyicholine and diphosphatidylglycerot has been studied. In terms of the lattice and continuum models of large ligand adsorption to membrane thermodynamic parameters for the protein-lipid complexes have been estimated. Lysozyme binding to liposomes containing more than 25 mot % of DPG has been found to be characterized by the positive cooperativity, originating, presumably, from the self-association of the bound protein. |
|---|