Partial purification of a nucleoside triphosphatase from the inner membrane of the chloroplast envelope of pea
| Autor: | Donald R. McCarty, Bruce R. Selman |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Azides
Chloroplasts Photochemistry viruses Detergents Biophysics Biology Biochemistry Chloroplast membrane chemistry.chemical_compound Adenosine Triphosphate Sodium fluoride Centrifugation Density Gradient Inner membrane Vanadate Sodium dodecyl sulfate Molecular Biology Polyacrylamide gel electrophoresis Adenosine Triphosphatases Plants Medicinal Chromatography Affinity Labels Fabaceae Vanadium Intracellular Membranes Chromatography Ion Exchange Nucleoside-Triphosphatase Phosphoric Monoester Hydrolases Ultrafiltration (renal) Membrane Solubility chemistry |
| Zdroj: | Archives of Biochemistry and Biophysics. 248:523-531 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(86)90505-9 |
| Popis: | A Mg2+-NTPase has been partially purified from the inner membrane of the pea chloroplast envelope. Isolated envelope membranes were solubilized with Triton X-100 and fractionated by DEAE-Sephadex chromatography, followed by ultrafiltration and sucrose density gradient centrifugation. An approximate 35-fold increase in the specific activity of the vanadate and sodium fluoride sensitive NTPase was obtained. Analysis of the partially purified NTPase by sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 37-kDa polypeptide that appeared to be associated with the activity. In support of this identification, it is demonstrated that the 37-kDa polypeptide can be photolabeled with 8-azido-ATP. |
| Databáze: | OpenAIRE |
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