Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification.
Open Access
- 1 March 1983
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 96 (3), 911-914
- https://doi.org/10.1083/jcb.96.3.911
Abstract
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.Keywords
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