Characteristics of tubulin aggregation by tubulin-binding proteins from brain and by synthetic polycations
ISSN: |
0020-711X
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798290879922831362 |
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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 |