Microsomal membrane proteins and vanadate-sensitive ATPase from Vicia faba root tips after clinostat treatment
Microsomal and soluble protein fractions from Vicia faba root tips were used for SDS-PAGE and Western-immunoblot analysis with anti-ubiquitin antibodies after 9 h clinostat treatment of the plants. In contrast to soluble proteins omnilateral gravistimulation (9 h) resulted in an enhanced proteolytic...
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 34(1996), 4 vom: 25. Juli, Seite 465-72 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
1996
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| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Membrane Proteins Plant Proteins Ubiquitins Adenosine Triphosphatases EC 3.6.1.- vanadate-sensitive ATPase Proton-Translocating ATPases EC 3.6.3.14 |
| Zusammenfassung: | Microsomal and soluble protein fractions from Vicia faba root tips were used for SDS-PAGE and Western-immunoblot analysis with anti-ubiquitin antibodies after 9 h clinostat treatment of the plants. In contrast to soluble proteins omnilateral gravistimulation (9 h) resulted in an enhanced proteolytic capacity for microsomal proteins. The increase of vanadate-sensitive ATPase activity was 83% after 9 h clinostat treatment, when the enzyme activity was measured directly after membrane preparation. Enhanced ATPase activity was correlated with the appearance of a polypeptide of about 100 kDa and its fragments (93 and 80 kDa). ATPases are not the only membrane bound proteins, which are changed during clinostat treatment, as several ubiquitinated polypeptides were also affected. A 1 h storage of microsomal fractions led to a shift of band intensities on ubiquitin-specific Western-blots. The demonstrated effect could not be observed, when fractions were isolated in the presence of protease inhibitors. In accordance with the polypeptide analysis omnilateral gravistimulation resulted in an enhanced capacity to degrade specific microsomal ubiquitin-conjugates, whereas the soluble ubiquitin-pool was not visibly affected |
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| Beschreibung: | Date Completed 17.07.1997 Date Revised 30.09.2020 published: Print Citation Status MEDLINE |
| ISSN: | 0981-9428 |