| Автор | Staudenbauer, Walter L. |
| Автор | Orr, Elisha |
| Дата выпуска | 1981 |
| dc.description | Novobiocin-Sepharose was prepared by coupling of novobiocin to Epoxy-activated Sepharose 6B and used as an affinity adsorbent. Four novobiocin-binding proteins were isolated from crude extracts of Escherichia coli with molecular weights of 105, 92, 85, and 40 kdal. The two larger proteins were identified as the A subunit (gyrA protein) and the B subunit (gyrB protein) of DNA gyrase (topoisomerase II). By this method the two gyrase components can be easily separated and purified in high yield. Although both proteins are involved in the ATP-dependent supercoiling of relaxed plasmid DNA, only the gyrB protein is required for catalyzing the cleavage of ATP. The gyrB protein ATPase activity is competitively inhibited by novobiocin and related coumarin antibiotics. ATP hydrolysis is unaffected by the addition of either gyrA protein or DNA but stimulated in the presence of both. |
| Формат | application.pdf |
| Издатель | Oxford University Press |
| Копирайт | © IRL Press Limited. |
| Тема | ENZYMOLOGY |
| Название | DNA gyrase: affinity chromatography on novobiocin-Sepharose and catalytic properties |
| Тип | research-article |
| Electronic ISSN | 1362-4962 |
| Print ISSN | 0305-1048 |
| Журнал | Nucleic Acids Research |
| Том | 9 |
| Первая страница | 3589 |
| Последняя страница | 3603 |
| Аффилиация | Max-Planck-Institut für Molekulare GenetikAbt. Schuster, D-1000 Berlin 33, GFR |
| Аффилиация | Orr Elisha; Department of Genetics, University of Leicester |
| Выпуск | 15 |
