Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1987970 | International Journal of Biological Macromolecules | 2007 | 6 Pages |
Abstract
The intent, in this work, was to isolate rat testis myosin II. Testis 40,000 × g × 40′ supernatant was frozen at −20 °C for 48 h and, after it was thawed and centrifuged. The precipitate, after washed twice, was enriched in three polypeptides bands: p205, p43 and one that migrated together with the front of the gel. These polypeptides were solubilized in pH 10.8 at 27 °C and separated in Sephacryl S-400 column. Three low weight polypeptides co-eluted together with p205. The p205 was marked with anti-myosin II, possess actin-stimulated Mg-ATPase activity and co-sedimented with F-actin in the absence, but not in the presence, of ATP. In the present study, we have been developing a method for purification of myosin II from rat testis.
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Authors
Decivaldo dos Santos Dias, Milton Vieira Coelho,