from the Atlantic Cod, Gadus morhua

Abstract. Assembly of brain microtubule proteins isolated from the Atlantic cod, Gadus morhua, was found to be much less sensitive to colchicine than assembly of bovine brain microtubules, which was completely inhibited by low colchicine concentrations (10 #M). The degree of disassembly by colchicin...

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Main Authors: Stability Acetylated, Cold-labile Brain Microtubules, Martin Billger, Margareta Wallin
Other Authors: The Pennsylvania State University CiteSeerX Archives
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Language:English
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Online Access:http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.283.1580
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spelling ftciteseerx:oai:CiteSeerX.psu:10.1.1.283.1580 2023-05-15T15:26:57+02:00 from the Atlantic Cod, Gadus morhua Stability Acetylated Cold-labile Brain Microtubules Martin Billger Margareta Wallin The Pennsylvania State University CiteSeerX Archives application/zip http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.283.1580 en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.283.1580 Metadata may be used without restrictions as long as the oai identifier remains attached to it. ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/c0/2f/J_Cell_Biol_1991_Apr_2_113(2)_331-338.tar.gz text ftciteseerx 2016-01-07T21:10:06Z Abstract. Assembly of brain microtubule proteins isolated from the Atlantic cod, Gadus morhua, was found to be much less sensitive to colchicine than assembly of bovine brain microtubules, which was completely inhibited by low colchicine concentrations (10 #M). The degree of disassembly by colchicine was also less for cod microtubules. The lack of colchicine effect was not caused by a lower affinity of colchicine to cod tubulin, as colchicine bound to cod tubulin with a dissociation constant, Kd, and a binding ratio close to that of bovine tubulin. Cod brain tubulin was highly acetylated and mainly detyrosinated, as opposed to bovine tubulin. When cod tubulin, purified by means of phosphocellulose chromatography, was assembled by addition of DMSO Text atlantic cod Gadus morhua Unknown
institution Open Polar
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language English
description Abstract. Assembly of brain microtubule proteins isolated from the Atlantic cod, Gadus morhua, was found to be much less sensitive to colchicine than assembly of bovine brain microtubules, which was completely inhibited by low colchicine concentrations (10 #M). The degree of disassembly by colchicine was also less for cod microtubules. The lack of colchicine effect was not caused by a lower affinity of colchicine to cod tubulin, as colchicine bound to cod tubulin with a dissociation constant, Kd, and a binding ratio close to that of bovine tubulin. Cod brain tubulin was highly acetylated and mainly detyrosinated, as opposed to bovine tubulin. When cod tubulin, purified by means of phosphocellulose chromatography, was assembled by addition of DMSO
author2 The Pennsylvania State University CiteSeerX Archives
format Text
author Stability Acetylated
Cold-labile Brain Microtubules
Martin Billger
Margareta Wallin
spellingShingle Stability Acetylated
Cold-labile Brain Microtubules
Martin Billger
Margareta Wallin
from the Atlantic Cod, Gadus morhua
author_facet Stability Acetylated
Cold-labile Brain Microtubules
Martin Billger
Margareta Wallin
author_sort Stability Acetylated
title from the Atlantic Cod, Gadus morhua
title_short from the Atlantic Cod, Gadus morhua
title_full from the Atlantic Cod, Gadus morhua
title_fullStr from the Atlantic Cod, Gadus morhua
title_full_unstemmed from the Atlantic Cod, Gadus morhua
title_sort from the atlantic cod, gadus morhua
url http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.283.1580
genre atlantic cod
Gadus morhua
genre_facet atlantic cod
Gadus morhua
op_source ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/c0/2f/J_Cell_Biol_1991_Apr_2_113(2)_331-338.tar.gz
op_relation http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.283.1580
op_rights Metadata may be used without restrictions as long as the oai identifier remains attached to it.
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