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Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes
Meiotic spindles isolated from surf clam oocytes to morphological purity are biochemically complex, consisting of many polypeptides. These proteins fall into two classes: (a) polypeptides that are apparently cytoplasmic proteins and are not specifically associated with the spindle; and (b) polypepti...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1980
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110549/ https://www.ncbi.nlm.nih.gov/pubmed/7189754 |
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collection | PubMed |
description | Meiotic spindles isolated from surf clam oocytes to morphological purity are biochemically complex, consisting of many polypeptides. These proteins fall into two classes: (a) polypeptides that are apparently cytoplasmic proteins and are not specifically associated with the spindle; and (b) polypeptides that are specifically associated with the spindle. A subset of the spindle-associated proteins, including a 250,000 mol wt component, remain with spindle tubulin through cycles of cold depolymerization and warm polymerization, showing that they are microtubule-associated proteins. |
format | Text |
id | pubmed-2110549 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1980 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21105492008-05-01 Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes J Cell Biol Articles Meiotic spindles isolated from surf clam oocytes to morphological purity are biochemically complex, consisting of many polypeptides. These proteins fall into two classes: (a) polypeptides that are apparently cytoplasmic proteins and are not specifically associated with the spindle; and (b) polypeptides that are specifically associated with the spindle. A subset of the spindle-associated proteins, including a 250,000 mol wt component, remain with spindle tubulin through cycles of cold depolymerization and warm polymerization, showing that they are microtubule-associated proteins. The Rockefeller University Press 1980-02-01 /pmc/articles/PMC2110549/ /pubmed/7189754 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 Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
title | Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
title_full | Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
title_fullStr | Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
title_full_unstemmed | Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
title_short | Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
title_sort | identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110549/ https://www.ncbi.nlm.nih.gov/pubmed/7189754 |