Related Experiment Videos
Ligatin from embryonic chick neural retina.
The Journal of Cell Biology
|March 1, 1979
Summary
Ligatin, a filamentous protein, was purified from chick neural retina. It functions as a baseplate for cell surface proteins in both retina and ileum.
Area of Science:
- Cell Biology
- Biochemistry
- Protein Structure
Background:
- Ligatin is a filamentous protein identified in rat ileum.
- Filamentous structures are present on embryonic chick neural retina plasma membranes.
Purpose of the Study:
- To purify ligatin from chick neural retina.
- To characterize ligatin's structure and function in the retina.
- To compare ligatin's function in retina and ileum.
Main Methods:
- Purification of ligatin from plasma membranes using Ca++ treatment, EGTA dialysis, and sieve chromatography.
- Electrophoresis and amino acid composition analysis of purified ligatin.
- In vitro polymerization of ligatin monomers with Ca++.
Main Results:
- Purified ligatin monomer (10,000 daltons) polymerizes into 3 nm filaments upon Ca++ addition.
- Retinal ligatin filaments are larger than 3 nm in vivo, suggesting association with other proteins.
- Ligatin in retina appears to serve as a baseplate for distinct cell surface proteins, unlike the beta-N-acetylhexosaminidase in ileum.
Conclusions:
- Ligatin is a conserved protein functioning as a cell surface baseplate in both neural retina and ileum.
- Ligatin facilitates the attachment of different proteins in different tissues.
- Further research is needed to identify the specific proteins associated with ligatin in the retina.