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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 b...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1983
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112400/ https://www.ncbi.nlm.nih.gov/pubmed/6833387 |
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collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2112400 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1983 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21124002008-05-01 Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification J Cell Biol Articles 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. The Rockefeller University Press 1983-03-01 /pmc/articles/PMC2112400/ /pubmed/6833387 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
title | Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
title_full | Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
title_fullStr | Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
title_full_unstemmed | Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
title_short | Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
title_sort | tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112400/ https://www.ncbi.nlm.nih.gov/pubmed/6833387 |