Isolation and characterization of Physarum profilin.
A protein that functionally resembles mammalian and Acanthamoeba profilins, has been purified from Physarum plasmodia. Physarum profilin consists of a single polypeptide with a molecular weight of 11,000-13,000. It has an isoelectric point of 5.35-5.40 under denaturing conditions. The amino acid composition of this protein is similar to those of profilins isolated from other sources. Physarum profilin prolongs the process of actin polymerization in a concentration-dependent fashion. This effect is much stronger for Physarum G-actin than for muscle G-actin.
D000199:Actins / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001704:Biopolymers; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003285:Contractile Proteins; D005656:Fungal Proteins / Q000302:isolation & purification*; D008840:Microfilament Proteins; D009124:Muscle Proteins / Q000302:isolation & purification; D010804:Physarum / Q000378:metabolism*; D051304:Profilins; D011506:Proteins / Q000302:isolation & purification*
D000199:Actins; D000596:Amino Acids; D001704:Biopolymers; D003285:Contractile Proteins; D005656:Fungal Proteins; D008840:Microfilament Proteins; D009124:Muscle Proteins; D051304:Profilins; D011506:Proteins