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01000caa a22002652 4500 |
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NLM114372071 |
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DE-627 |
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20250202194559.0 |
| 007 |
tu |
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231222s1996 xx ||||| 00| ||eng c |
| 028 |
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2 |
|a pubmed25n0382.xml
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|a (DE-627)NLM114372071
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|a (NLM)11539386
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Bramer, M
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Microsomal membrane proteins and vanadate-sensitive ATPase from Vicia faba root tips after clinostat treatment
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| 264 |
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1 |
|c 1996
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 17.07.1997
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| 500 |
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|a Date Revised 30.09.2020
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| 500 |
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a 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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| 650 |
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Membrane Proteins
|2 NLM
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| 650 |
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7 |
|a Plant Proteins
|2 NLM
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| 650 |
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7 |
|a Ubiquitins
|2 NLM
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| 650 |
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7 |
|a Adenosine Triphosphatases
|2 NLM
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| 650 |
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7 |
|a EC 3.6.1.-
|2 NLM
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| 650 |
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7 |
|a vanadate-sensitive ATPase
|2 NLM
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| 650 |
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7 |
|a EC 3.6.1.-
|2 NLM
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| 650 |
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7 |
|a Proton-Translocating ATPases
|2 NLM
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| 650 |
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7 |
|a EC 3.6.3.14
|2 NLM
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| 700 |
1 |
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|a Hunte, C
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schulz, M
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schnabl, H
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 34(1996), 4 vom: 25. Juli, Seite 465-72
|w (DE-627)NLM098178261
|x 0981-9428
|7 nnns
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| 773 |
1 |
8 |
|g volume:34
|g year:1996
|g number:4
|g day:25
|g month:07
|g pages:465-72
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| 912 |
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|a GBV_USEFLAG_A
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| 912 |
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|a SYSFLAG_A
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|a AR
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| 952 |
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|d 34
|j 1996
|e 4
|b 25
|c 07
|h 465-72
|