Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting
| ISSN: |
0006-291X
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| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
Physics
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798292241305829376 |
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| autor | Rendon, A. Filliol, D. Jancsik, V. |
| autorsonst | Rendon, A. Filliol, D. Jancsik, V. |
| book_url | http://dx.doi.org/10.1016/0006-291X(87)90435-9 |
| datenlieferant | nat_lic_papers |
| fussnote | Axonal transport of mitochondria is a microtubule-associated movement. Microtubule-mitochondria interactions were studied in vitro using organelles isolated from rat brain. Thanks to the ligand blotting method we were able to show two mitochondrial membrane proteins with apparent molecular masses of 30 kDa and 60 kDa that bind microtubule-associated proteins. The binding of the 30 kDa protein has an apparent Kd of 8 x10^-^8M. Digitonin fractionation of mitochondria reveals a bimodal localization of the 30 kDa and the 60 kDa proteins within the outer membrane. The data suggest that these polypeptides could participate to the interactions observed in situ between microtubules and mitochondria. |
| hauptsatz | hsatz_simple |
| identnr | NLZ184122104 |
| issn | 0006-291X |
| journal_name | Biochemical and Biophysical Research Communications |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 149 (1987), S. 776-783 |
| search_space | articles |
| shingle_author_1 | Rendon, A. Filliol, D. Jancsik, V. |
| shingle_author_2 | Rendon, A. Filliol, D. Jancsik, V. |
| shingle_author_3 | Rendon, A. Filliol, D. Jancsik, V. |
| shingle_author_4 | Rendon, A. Filliol, D. Jancsik, V. |
| shingle_catch_all_1 | Rendon, A. Filliol, D. Jancsik, V. Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting 0006-291X 0006291X Elsevier |
| shingle_catch_all_2 | Rendon, A. Filliol, D. Jancsik, V. Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting 0006-291X 0006291X Elsevier |
| shingle_catch_all_3 | Rendon, A. Filliol, D. Jancsik, V. Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting 0006-291X 0006291X Elsevier |
| shingle_catch_all_4 | Rendon, A. Filliol, D. Jancsik, V. Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting 0006-291X 0006291X Elsevier |
| shingle_title_1 | Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting |
| shingle_title_2 | Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting |
| shingle_title_3 | Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting |
| shingle_title_4 | Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:45:22.855Z |
| titel | Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting |
| titel_suche | Microtubule-associated proteins bind to 30 kDa and 60 kDa proteins of rat brain mitochondria: Visualization by ligand blotting Axonal transport of mitochondria is a microtubule-associated movement. Microtubule-mitochondria interactions were studied in vitro using organelles isolated from rat brain. Thanks to the ligand blotting method we were able to show two mitochondrial membrane proteins with apparent molecular masses of 30 kDa and 60 kDa that bind microtubule-associated proteins. The binding of the 30 kDa protein has an apparent Kd of 8 x10^-^8M. Digitonin fractionation of mitochondria reveals a bimodal localization of the 30 kDa and the 60 kDa proteins within the outer membrane. The data suggest that these polypeptides could participate to the interactions observed in situ between microtubules and mitochondria. |
| topic | W V U |
| uid | nat_lic_papers_NLZ184122104 |