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Selective extraction of desmosomal proteins by low ionic strength media
Biochimica Et Biophysica Acta
|July 25, 1979
Summary
Low ionic strength extraction removes significant high molecular weight proteins from desmosomes. This process yields residual structures, impacting protein composition without drastic ultrastructural changes.
Area of Science:
- Cell biology
- Biochemistry
Background:
- Desmosomes are crucial intercellular junctions involved in cell adhesion.
- Understanding desmosome protein composition is key to deciphering their function.
Purpose of the Study:
- To investigate the effects of low ionic strength extraction on desmosome protein composition.
- To identify specific proteins removed during this extraction process.
Main Methods:
- Desmosomes were isolated using an acidic buffer.
- Extraction was performed at low ionic strength.
- Protein composition and ultrastructure of residual desmosomes were analyzed.
Main Results:
- Low ionic strength extraction removed over 35% of desmosome protein.
- Two specific polypeptide chains (210,000 and 230,000 Da) were identified as major components removed.
- Residual desmosomes exhibited only subtle changes in ultrastructure.
Conclusions:
- Low ionic strength media effectively deplete desmosomes of high molecular weight proteins.
- This extraction method yields residual desmosome structures with altered protein profiles.