| Autor: |
Thomas Börner, Ralf Boldt, Claus Schnarrenberger, Birgit Pelzer-Reith |
| Rok vydání: |
1994 |
| Předmět: |
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| Zdroj: |
Journal of Plant Physiology. 144:282-286 |
| ISSN: |
0176-1617 |
| DOI: |
10.1016/s0176-1617(11)81188-0 |
| Popis: |
Summary The plastidic and cytosolic aldolases were purified from green leaves of barley ( Hordeum vulgare L. cv. Salome) to almost homogeneity on DEAE-Fractogel, P-Cellulose and Fractogel AX 300 (HPCL). The two homotetrameric aldolases have molecular masses of the subunits of 36 and 38 kDa, respectively, and Km(FBP) values of 10 μM and 2 μM, respectively. Both enzymes were extremely unstable. Loss of activity could partly be prevented by the addition of the protease inhibitors leupeptin or PMSF. In white leaf tissue of the plastome mutant «calbostrians» of barley the activity of the plastidic isoenzyme is strongly reduced while the activity of the cytosolic isoenzyme was little affected. Western and Northern blot analyses indicated a strong reduction in protein content and in mRNA level of the plastidic but not of the cytosolic aldolase. The protein content and mRNA level of the cytosolic aldolase were similar in white and green leaf tissue. The results support the hypothesis that a plastidic signal causes the repression of the nuclear-encoded plastidic aldolase on a transcriptional level but does not affect the expression of the cytosolic aldolase. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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