Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations

Miyatake, K. ; Flavin, M.

Amsterdam : Elsevier
ISSN:
0020-711X
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Type of Medium:
Electronic Resource
URL:
_version_ 1798290879922831362
autor Miyatake, K.
Flavin, M.
autorsonst Miyatake, K.
Flavin, M.
book_url http://linkinghub.elsevier.com/retrieve/pii/0020-711X(83)90020-4
datenlieferant nat_lic_papers
fussnote 1. A basic fraction from brain cytosol was found to contain two or more tubulin-binding proteins, able to induce aggregation of tubulin accompanied by hydrolysis of GTP.2. In some respects tubulin aggregation by the brain proteins was similar to its aggregation by polylysine.3. The burst of GTP hydrolysis accompanying tubulin aggregation by polylysine had the following characteristics: enhanced by salt and abolished by low temperature; not stoichiometric with the amount of tubulin precipitated and actually maximal at relatively low polylysine concentration; uncoupled temporally from aggregation, which occurred over a much shorter interval.
hauptsatz hsatz_simple
identnr NLZ186250843
issn 0020-711X
journal_name International Journal of Biochemistry
materialart 1
package_name Elsevier
publikationsort Amsterdam
publisher Elsevier
reference 15 (1983), S. 1305-1312
search_space articles
shingle_author_1 Miyatake, K.
Flavin, M.
shingle_author_2 Miyatake, K.
Flavin, M.
shingle_author_3 Miyatake, K.
Flavin, M.
shingle_author_4 Miyatake, K.
Flavin, M.
shingle_catch_all_1 Miyatake, K.
Flavin, M.
Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
0020-711X
0020711X
Elsevier
shingle_catch_all_2 Miyatake, K.
Flavin, M.
Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
0020-711X
0020711X
Elsevier
shingle_catch_all_3 Miyatake, K.
Flavin, M.
Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
0020-711X
0020711X
Elsevier
shingle_catch_all_4 Miyatake, K.
Flavin, M.
Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
0020-711X
0020711X
Elsevier
shingle_title_1 Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
shingle_title_2 Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
shingle_title_3 Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
shingle_title_4 Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
sigel_instance_filter dkfz
geomar
wilbert
ipn
albert
fhp
source_archive Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
timestamp 2024-05-06T08:23:45.050Z
titel Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
titel_suche Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
1. A basic fraction from brain cytosol was found to contain two or more tubulin-binding proteins, able to induce aggregation of tubulin accompanied by hydrolysis of GTP.2. In some respects tubulin aggregation by the brain proteins was similar to its aggregation by polylysine.3. The burst of GTP hydrolysis accompanying tubulin aggregation by polylysine had the following characteristics: enhanced by salt and abolished by low temperature; not stoichiometric with the amount of tubulin precipitated and actually maximal at relatively low polylysine concentration; uncoupled temporally from aggregation, which occurred over a much shorter interval.
topic W
V
uid nat_lic_papers_NLZ186250843