Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification.
The light chains (LCa and LCb) of bovine brain clathrin are resistant to heat denaturation by boiling, a property shared by tropomyosin (Bailey, K., 1948, Biochem. J., 43:271-281). Light chains were partially purified by boiling and centrifugation of a Tris-extract of crude membranes prepared from bovine brains (Keen, J. H., M. C. Willingham, and I. H. Pastan, 1979, Cell., 16:303-312). Contaminant polypeptides were then removed by size-exclusion high-pressure liquid chromatography. The purified light chains were separated from each other by using an immunoaffinity column prepared from a monoclonal antibody CVC.7 specific for LCa and not LCb.
D000818:Animals; D000911:Antibodies, Monoclonal; D001923:Brain Chemistry; D002417:Cattle; D002498:Centrifugation; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D002966:Clathrin; D006358:Hot Temperature; D008565:Membrane Proteins / Q000276:immunology / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D002966:Clathrin; D008565:Membrane Proteins