The presence of soluble carbonic anhydrase in the thylakoid lumen of chloroplasts from Arabidopsis leaves |
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Authors: | Tat&rsquo yana Fedorchuk,Natalia RudenkoLyudmila Ignatova,Boris Ivanov |
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Affiliation: | Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino 142290, Russia |
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Abstract: | Supernatant obtained after high-speed centrifugation of disrupted thylakoids that had been washed free from extrathylakoid carbonic anhydrases demonstrated carbonic anhydrase activity that was inhibited by the specific inhibitors acetazolamide and ethoxyzolamide. A distinctive feature of the effect of Triton X-100 on this activity also suggested that the source of the activity is a soluble protein. Native electrophoresis of a preparation obtained using chromatography with agarose/mafenide as an affinity sorbent revealed one protein band with carbonic anhydrase activity. The same protein was revealed in a mutant deficient in soluble stromal carbonic anhydrase β-CA1, and this indicated that the newly revealed carbonic anhydrase is not a product of the At3g01500 gene. These data imply the presence of soluble carbonic anhydrase in the thylakoid lumen of higher plants. |
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Keywords: | AZ, acetazolamide BSA, bovine serum albumin CA, carbonic anhydrase Chl, chlorophyll DTT, 1,4-dithio-dl-threitol EZ, ethoxyzolamide PAAG, polyacrylamide gel PMSF, phenylmethylsulfonyl fluoride PSI, photosystem I PSII, photosystem II Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase WT, wild type β1-mut, the mutant deficient in soluble stromal carbonic anhydrase |
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