Abstract
Human erythrocyte ghosts were incubated with the proteolytic enzyme pronase under isotonic (iso-human erythrocyte ghosts) or hypotonic (hypohuman erythrocyte ghosts) conditions. Gel electrophoresis and electron microscope (freeze-etching) studies revealed that most of the erythrocyte membrane polypeptides were hydrolyzed by pronase under hypotonic conditions. Sendai virus readily agglutinated both pronase-digested iso-human erythrocyte ghosts and hypo-human erythrocyte ghosts but was able to fuse only iso-human erythrocyte ghosts. Iso- and hypo-human erythrocyte ghosts were fused by the non-viral fusogenic agent glyceromonooleate. Freeze-etching studies revealed that during fusion the membranes of pronase-digested human erythrocyte ghosts are intermixed.
Original language | English |
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Pages (from-to) | 282-294 |
Number of pages | 13 |
Journal | Biochimica et Biophysica Acta - Biomembranes |
Volume | 551 |
Issue number | 2 |
DOIs | |
State | Published - 8 Mar 1979 |
Keywords
- (Erythrocyte ghost
- Membrane fusion
- Pronase digestion
- Sendai virus)