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Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification.

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The Journal of Cell Biology, 01 Mar 1983, 96(3):911-914
https://doi.org/10.1083/jcb.96.3.911 PMID: 6833387 PMCID: PMC2112400

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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.

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J Cell Biol. 1983 Mar 1; 96(3): 911–914.
PMCID: PMC2112400
PMID: 6833387

Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification

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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.

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Selected References

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