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Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg
A KCl-soluble protein fraction can be extracted from the water-insoluble residue of the homogenate of sea urchin eggs which contains three major components separable by ultracentrifugation. When the extract is stirred in acetone or distilled water, a fibrous precipitate appears which has a strong bi...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1962
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195184/ https://www.ncbi.nlm.nih.gov/pubmed/14496152 |
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author | Sakai, Hikoichi |
author_facet | Sakai, Hikoichi |
author_sort | Sakai, Hikoichi |
collection | PubMed |
description | A KCl-soluble protein fraction can be extracted from the water-insoluble residue of the homogenate of sea urchin eggs which contains three major components separable by ultracentrifugation. When the extract is stirred in acetone or distilled water, a fibrous precipitate appears which has a strong birefringence positive in the direction of the long axis. When the fraction is squirted through a slender tubing, it precipitates in the form of a thread. The thread model contracts vigorously under the action of di-, tri-, and tetravalent metal ions; the contraction can be reversed by EDTA. The contraction and the elongation of the thread model can be repeated many times. The thread model contracts also in the presence of dehydroascorbic acid, cystine, oxidized glutathione, or other oxidizing agents, and this contraction is reversed by reducing agents such as cysteine or ascorbic acid. When —SH groups of the thread model are blocked by various —SH reagents, the contraction by metal ions is inhibited to some extent. As mechanisms of the contraction, electrostatic forces between metal ions and negative charges of the thread model are essential for metal ion-induced contraction and oxidation of —SH groups of the thread model for the contraction by oxidizing reagents. |
format | Text |
id | pubmed-2195184 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1962 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21951842008-04-23 Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg Sakai, Hikoichi J Gen Physiol Article A KCl-soluble protein fraction can be extracted from the water-insoluble residue of the homogenate of sea urchin eggs which contains three major components separable by ultracentrifugation. When the extract is stirred in acetone or distilled water, a fibrous precipitate appears which has a strong birefringence positive in the direction of the long axis. When the fraction is squirted through a slender tubing, it precipitates in the form of a thread. The thread model contracts vigorously under the action of di-, tri-, and tetravalent metal ions; the contraction can be reversed by EDTA. The contraction and the elongation of the thread model can be repeated many times. The thread model contracts also in the presence of dehydroascorbic acid, cystine, oxidized glutathione, or other oxidizing agents, and this contraction is reversed by reducing agents such as cysteine or ascorbic acid. When —SH groups of the thread model are blocked by various —SH reagents, the contraction by metal ions is inhibited to some extent. As mechanisms of the contraction, electrostatic forces between metal ions and negative charges of the thread model are essential for metal ion-induced contraction and oxidation of —SH groups of the thread model for the contraction by oxidizing reagents. The Rockefeller University Press 1962-01-01 /pmc/articles/PMC2195184/ /pubmed/14496152 Text en Copyright © Copyright, 1962, by The Rockefeller Institute Press 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 | Article Sakai, Hikoichi Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg |
title | Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg |
title_full | Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg |
title_fullStr | Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg |
title_full_unstemmed | Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg |
title_short | Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg : IV. Contractile properties of the thread model of KCl-soluble protein from the sea urchin egg |
title_sort | studies on sulfhydryl groups during cell division of sea urchin egg : iv. contractile properties of the thread model of kcl-soluble protein from the sea urchin egg |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195184/ https://www.ncbi.nlm.nih.gov/pubmed/14496152 |
work_keys_str_mv | AT sakaihikoichi studiesonsulfhydrylgroupsduringcelldivisionofseaurchineggivcontractilepropertiesofthethreadmodelofkclsolubleproteinfromtheseaurchinegg |