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Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia
A high molecular weight actin-binding protein was isolated from the Physarum polycephalum plasmodia. The protein ( HMWP ) shares many properties with other high molecular weight actin-binding proteins such as spectrin, actin-binding protein from macrophages, and filamin. It has a potent activity to...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1984
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113185/ https://www.ncbi.nlm.nih.gov/pubmed/6725393 |
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collection | PubMed |
description | A high molecular weight actin-binding protein was isolated from the Physarum polycephalum plasmodia. The protein ( HMWP ) shares many properties with other high molecular weight actin-binding proteins such as spectrin, actin-binding protein from macrophages, and filamin. It has a potent activity to cross-link F-actin into a gel-like structure. Its cross-linking activity does not depend on calcium concentrations. Hydrodynamic studies have revealed that the protein is in the monomeric state of a polypeptide chain with molecular weight of approximately 230,000 in a high ionic strength solvent, while it self-associates into a dimer under physiological ionic conditions. Electron microscopic examinations of HMWP have shown that the monomer particle observed in a high ionic strength solvent is rod shaped with the two-stranded morphology very similar to that of spectrin. On the other hand, under physiological ionic conditions, the HMWP dimer shows the dumb-bell shape with two globular domains connected with a thin flexible strand. |
format | Text |
id | pubmed-2113185 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1984 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21131852008-05-01 Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia J Cell Biol Articles A high molecular weight actin-binding protein was isolated from the Physarum polycephalum plasmodia. The protein ( HMWP ) shares many properties with other high molecular weight actin-binding proteins such as spectrin, actin-binding protein from macrophages, and filamin. It has a potent activity to cross-link F-actin into a gel-like structure. Its cross-linking activity does not depend on calcium concentrations. Hydrodynamic studies have revealed that the protein is in the monomeric state of a polypeptide chain with molecular weight of approximately 230,000 in a high ionic strength solvent, while it self-associates into a dimer under physiological ionic conditions. Electron microscopic examinations of HMWP have shown that the monomer particle observed in a high ionic strength solvent is rod shaped with the two-stranded morphology very similar to that of spectrin. On the other hand, under physiological ionic conditions, the HMWP dimer shows the dumb-bell shape with two globular domains connected with a thin flexible strand. The Rockefeller University Press 1984-05-01 /pmc/articles/PMC2113185/ /pubmed/6725393 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 Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia |
title | Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia |
title_full | Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia |
title_fullStr | Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia |
title_full_unstemmed | Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia |
title_short | Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia |
title_sort | isolation and characterization of a high molecular weight actin-binding protein from physarum polycephalum plasmodia |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113185/ https://www.ncbi.nlm.nih.gov/pubmed/6725393 |