| Autor: |
Dias Ddos S; Universidade Federal de Uberlândia, Instituto de Genética e Bioquímica, Av. Pará 1720, bloco 2E39b, Bairro Umuarama, Uberlândia, Minas Gerais 38.400-902, Brazil., Coelho MV |
| Jazyk: |
angličtina |
| Zdroj: |
International journal of biological macromolecules [Int J Biol Macromol] 2007 Oct 01; Vol. 41 (4), pp. 475-80. Date of Electronic Publication: 2007 Jun 23. |
| DOI: |
10.1016/j.ijbiomac.2007.06.007 |
| Abstrakt: |
The intent, in this work, was to isolate rat testis myosin II. Testis 40,000 x g x 40' supernatant was frozen at -20 degrees 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 degrees 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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