Fischer-Schliebs, Elke ; Ball, Erika ; Berndt, Ekkehart ; Besemfelder-Butz, Eva ; Binzel, Marla L. ; Drobny, Martina ; Mühlenhoff, Dagmar ; Müller, Mathias L. ; Rakowski, Krzysztof ; Ratajczak, Rafael (1997)
Differential Immunological Cross-Reactions with Antisera against the V-ATPase of Kalanchoë daigremontiana Reveal Structural Differences of V-ATPase Subunits of Different Plant Species.
In: Biological chemistry, 378 (10)
doi: 10.1515/bchm.1997.378.10.1131
Article
Abstract
Two antisera (ATP88 and ATP95) raised against the V-ATPase holoenzyme of Kalanchoe daigremontianawere tested for their cross-reactivity with subunits ofV-ATPases from other plant species. V-ATPases fromKalanchoe blossfeldiana, Mesembryanthemum crys-tallinum, Nicotians tabacum, Lycopersicon esculentum, Citrus limon, Lemna gibba, Hordeum vulgäre and Zea mays were immunoprecipitated with an antiserumagainst the catalytic V-ATPase subunit A of M. crystal-linum. As shown by silver staining and Western blotanalysis with ATP88, subunits A, B, C, D and c werepresent in all immunoprecipitated V-ATPases. In contrast, ATP95 recognized the whole set of subunits onlyin K. blossfeldiana, M. crystallinum, H. vulgäre and Z.mays. This differential cross reactivity of ATP95 indicates the presence of structural differences of certainV-ATPase subunits. Based on the Bafilomycin A1-sen-sitive ATPase activity of tonoplast enriched vesicles, and on the amount of V-ATPase solubilized and immunoprecipitated, the specific ATP-hydrolysis activity ofthe V-ATPases under test was determined. The structural differences correlate with the ability of V-ATPases from different species to hydrolyze ATP atone given assay condition for ATP-hydrolysis measu-rements. Interestingly V-ATPases showing crossreactivity of subunits A, B, C, D and c with ATP95 showedhigher rates of specific ATP hydrolysis compared to V-ATPases containing subunits which were not labeledby 95. Thus, V-ATPases with high turnover rates in our assay conditions may show common structuralcharacteristics which separate them from ATPases with low turnover rates.
| Item Type: | Article |
|---|---|
| Erschienen: | 1997 |
| Creators: | Fischer-Schliebs, Elke ; Ball, Erika ; Berndt, Ekkehart ; Besemfelder-Butz, Eva ; Binzel, Marla L. ; Drobny, Martina ; Mühlenhoff, Dagmar ; Müller, Mathias L. ; Rakowski, Krzysztof ; Ratajczak, Rafael |
| Type of entry: | Bibliographie |
| Title: | Differential Immunological Cross-Reactions with Antisera against the V-ATPase of Kalanchoë daigremontiana Reveal Structural Differences of V-ATPase Subunits of Different Plant Species |
| Language: | English |
| Date: | 1 October 1997 |
| Publisher: | De Gruyter |
| Journal or Publication Title: | Biological chemistry |
| Volume of the journal: | 378 |
| Issue Number: | 10 |
| DOI: | 10.1515/bchm.1997.378.10.1131 |
| Abstract: | Two antisera (ATP88 and ATP95) raised against the V-ATPase holoenzyme of Kalanchoe daigremontianawere tested for their cross-reactivity with subunits ofV-ATPases from other plant species. V-ATPases fromKalanchoe blossfeldiana, Mesembryanthemum crys-tallinum, Nicotians tabacum, Lycopersicon esculentum, Citrus limon, Lemna gibba, Hordeum vulgäre and Zea mays were immunoprecipitated with an antiserumagainst the catalytic V-ATPase subunit A of M. crystal-linum. As shown by silver staining and Western blotanalysis with ATP88, subunits A, B, C, D and c werepresent in all immunoprecipitated V-ATPases. In contrast, ATP95 recognized the whole set of subunits onlyin K. blossfeldiana, M. crystallinum, H. vulgäre and Z.mays. This differential cross reactivity of ATP95 indicates the presence of structural differences of certainV-ATPase subunits. Based on the Bafilomycin A1-sen-sitive ATPase activity of tonoplast enriched vesicles, and on the amount of V-ATPase solubilized and immunoprecipitated, the specific ATP-hydrolysis activity ofthe V-ATPases under test was determined. The structural differences correlate with the ability of V-ATPases from different species to hydrolyze ATP atone given assay condition for ATP-hydrolysis measu-rements. Interestingly V-ATPases showing crossreactivity of subunits A, B, C, D and c with ATP95 showedhigher rates of specific ATP hydrolysis compared to V-ATPases containing subunits which were not labeledby 95. Thus, V-ATPases with high turnover rates in our assay conditions may show common structuralcharacteristics which separate them from ATPases with low turnover rates. |
| Divisions: | 10 Department of Biology 10 Department of Biology > Botanischer Garten |
| Date Deposited: | 19 Nov 2008 16:02 |
| Last Modified: | 11 Aug 2023 14:25 |
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