Abstract
The ratio of low-field amplitudes of weakly and strongly immobilized signals of ESR spectra of a maleimide spin label bound to erythrocyte membranes (hw/hs) increases progressively during incubation at 37δC. This increase is due to the 'self-digestion' of membrane proteins by endogenous proteinases and is attenuated by proteinase inhibitors. Digestion of membranes with chymotrypsin also increases the hw/hs, ratio. These results suggest a need for a careful interpretation of data from spin-labeled membrane proteins, especially in experiments involving prolonged incubations of membrane preparations when the proteolytic effects may be significant.
Original language | English (US) |
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Pages (from-to) | 175-178 |
Number of pages | 4 |
Journal | BBA - Biomembranes |
Volume | 821 |
Issue number | 2 |
DOIs | |
State | Published - Dec 5 1985 |
Externally published | Yes |
Keywords
- ESR
- Erythrocyte membrane
- Maleimide spin label
- Proteolysis
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology