Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules
A cold-labile fraction of microtubules with unusual properties was isolated from the brain of the Atlantic cod (Gadus morhua). The yield was low, approximately six times lower than that for bovine brain microtubules. This was mainly caused by the presence of a large amount of cold-stable microtubule...
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Canadian Science Publishing
1989
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crcansciencepubl:10.1139/o89-117 2023-12-17T10:27:02+01:00 Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules Strömberg, E. Serrano, L. Avila, J. Wallin, M. 1989 http://dx.doi.org/10.1139/o89-117 http://www.nrcresearchpress.com/doi/pdf/10.1139/o89-117 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Biochemistry and Cell Biology volume 67, issue 11-12, page 791-800 ISSN 0829-8211 1208-6002 Cell Biology Molecular Biology Biochemistry journal-article 1989 crcansciencepubl https://doi.org/10.1139/o89-117 2023-11-19T13:38:40Z A cold-labile fraction of microtubules with unusual properties was isolated from the brain of the Atlantic cod (Gadus morhua). The yield was low, approximately six times lower than that for bovine brain microtubules. This was mainly caused by the presence of a large amount of cold-stable microtubules, which were not broken down during the disassembly step in the temperature-dependent assembly–disassembly isolation procedure and were therefore lost. The isolated cold-labile cod microtubules contained usually only a low amount of microtubule-associated proteins (MAPs). Three high molecular mass proteins were found, of which one was recognized as MAP2. Cod MAP2 differed from mammalian brain MAP2; it was not heat stable and had a slightly higher molecular mass. In contrast to mammalian MAPs, MAP1 was not found in the cold-labile fraction of microtubules. A new heat-labile MAP of higher molecular mass (400 kilodaltons) was however present, as well as a heat-stable protein of slightly lower molecular mass than MAP2. These MAPs showed similar tubulin-binding characteristics as bovine brain MAPs, since they coassembled with taxol-assembled bovine brain microtubules consisting of pure bovine tubulin. In spite of the fact that Ca 2+ bound equally to cod and porcine tubulins, it did not inhibit cod microtubule assembly even at high concentrations (> 1 mM). In contrast, rings, spirals, and macrotubules were formed. The results show that there are major differences between this fraction of cod microtubules and microtubules from mammalian brain.Key words: microtubules, microtubule-associated proteins, calcium, cod. Article in Journal/Newspaper atlantic cod Gadus morhua Canadian Science Publishing (via Crossref) Biochemistry and Cell Biology 67 11-12 791 800 |
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Open Polar |
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Canadian Science Publishing (via Crossref) |
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crcansciencepubl |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry Strömberg, E. Serrano, L. Avila, J. Wallin, M. Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
A cold-labile fraction of microtubules with unusual properties was isolated from the brain of the Atlantic cod (Gadus morhua). The yield was low, approximately six times lower than that for bovine brain microtubules. This was mainly caused by the presence of a large amount of cold-stable microtubules, which were not broken down during the disassembly step in the temperature-dependent assembly–disassembly isolation procedure and were therefore lost. The isolated cold-labile cod microtubules contained usually only a low amount of microtubule-associated proteins (MAPs). Three high molecular mass proteins were found, of which one was recognized as MAP2. Cod MAP2 differed from mammalian brain MAP2; it was not heat stable and had a slightly higher molecular mass. In contrast to mammalian MAPs, MAP1 was not found in the cold-labile fraction of microtubules. A new heat-labile MAP of higher molecular mass (400 kilodaltons) was however present, as well as a heat-stable protein of slightly lower molecular mass than MAP2. These MAPs showed similar tubulin-binding characteristics as bovine brain MAPs, since they coassembled with taxol-assembled bovine brain microtubules consisting of pure bovine tubulin. In spite of the fact that Ca 2+ bound equally to cod and porcine tubulins, it did not inhibit cod microtubule assembly even at high concentrations (> 1 mM). In contrast, rings, spirals, and macrotubules were formed. The results show that there are major differences between this fraction of cod microtubules and microtubules from mammalian brain.Key words: microtubules, microtubule-associated proteins, calcium, cod. |
format |
Article in Journal/Newspaper |
author |
Strömberg, E. Serrano, L. Avila, J. Wallin, M. |
author_facet |
Strömberg, E. Serrano, L. Avila, J. Wallin, M. |
author_sort |
Strömberg, E. |
title |
Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules |
title_short |
Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules |
title_full |
Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules |
title_fullStr |
Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules |
title_full_unstemmed |
Unusual properties of a cold-labile fraction of Atlantic cod ( Gadus morhua ) brain microtubules |
title_sort |
unusual properties of a cold-labile fraction of atlantic cod ( gadus morhua ) brain microtubules |
publisher |
Canadian Science Publishing |
publishDate |
1989 |
url |
http://dx.doi.org/10.1139/o89-117 http://www.nrcresearchpress.com/doi/pdf/10.1139/o89-117 |
genre |
atlantic cod Gadus morhua |
genre_facet |
atlantic cod Gadus morhua |
op_source |
Biochemistry and Cell Biology volume 67, issue 11-12, page 791-800 ISSN 0829-8211 1208-6002 |
op_rights |
http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/o89-117 |
container_title |
Biochemistry and Cell Biology |
container_volume |
67 |
container_issue |
11-12 |
container_start_page |
791 |
op_container_end_page |
800 |
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1785578806488072192 |