Beta-actinin-like protein from plasmodium.
A beta-actinin-like protein was isolated from plasmodia of the slime mold. The chain weight was the same as that of actin (43,000), but the amino acid composition was significantly different. The action of plasmodium beta-actinin on actin was the same as that of beta-actinin from rabbit skeletal muscle: inhibition of the recombination of F-actin fragments; formation of Mg polymer; inhibition of interfilamental interaction of F-actin and retardation of depolymerization of F-actin. The only difference observed was its sensitivity to trypsin: plasmodium actinin was less quickly digested by trypsin than rabbit beta-actinin.
D000185:Actinin / Q000302:isolation & purification / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002942:Circular Dichroism; D046911:Macromolecular Substances; D008274:Magnesium; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification; D009235:Myxomycetes / Q000032:analysis*; D010804:Physarum / Q000032:analysis* / Q000378:metabolism; D010961:Plasmodium / Q000032:analysis* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D000199:Actins; D000596:Amino Acids; D046911:Macromolecular Substances; D009124:Muscle Proteins; D000185:Actinin; D008274:Magnesium