Purification and partial characterization of myosin II from rat testis.
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.
Dias
Decivaldo dos Santos
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
Milton Vieira
MV
D000199:Actins / Q000378:metabolism / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008297:Male; D008970:Molecular Weight; D024462:Myosin Type II / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D012995:Solubility; D013696:Temperature; D013737:Testis / Q000737:chemistry*
D000199:Actins; D000251:Adenosine Triphosphatases; D024462:Myosin Type II