Actin from diploid and haploid cells of the myxomycete Physarum flavicomum--comparison with skeletal muscle actin.
Glycerinated diploid microplasmodia of Physarum flavicomum exhibited ATP-dependent contractility typical of actomyosin controlled systems. Actin was isolated from microplasmodia, haploid amoebae-swarm cells, and rabbit skeletal muscle, by classical methods as well as ATP-DEAE cellulose chromatography, and isoelectric focusing. Actins from all three sources had isoelectric points in the pH 6.5-7.0 range, and behaved similarly during the various isolation procedures. SDS-gel electrophoresis revealed that the actin from microplasmodia and muscle had a molecule weight of about 46,000 daltons while the amoebae-swarm cells possessed proteins of molecular weights of about 46,000 and 51,000 daltons.
D000199:Actins / Q000032:analysis*; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D004171:Diploidy; D005656:Fungal Proteins / Q000032:analysis*; D006238:Haploidy; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D010804:Physarum / Q000032:analysis*; D011817:Rabbits
D000199:Actins; D005656:Fungal Proteins