The coexistence of vesiculation and the self-digestion process during incubation (37 degrees C, several hours) of bovine erythrocyte ghosts in the presence or absence of protease inhibitors was studied. The release of vesicles and proteolytic protein fragments into supernatants of membrane suspensions was analysed employing turbidimetric and nephelometric methods, protein concentration measurement and exposed amino group determination. Vesiculation seems to be independent of self-digestion. A model of membrane protein loss during ghost incubation is proposed and discussed.
|Idioma original||English (US)|
|Número de páginas||8|
|Estado||Published - 1988|
|Publicado de forma externa||Sí|
ASJC Scopus subject areas
- Aquatic Science
- Cell Biology