title: Lack of nucleotide cleavage on the binding of G-actin-ATP to plasma gelsolin.
abstract: G-Actin-ATP bound to plasma gelsolin to form a 2:1 complex. The complex contained approximately equivalent amounts of nucleotide and actin. More than 84% of this nucleotide was ATP. Half of the bound nucleotide was displaced by cold chase and the remainder did not exchange, implying that the two actins in the complex are not equivalent.
mesh_terms: D000199:Actins / Q000097:blood*; D000244:Adenosine Diphosphate / Q000097:blood; D000255:Adenosine Triphosphate / Q000097:blood*; D000818:Animals; D002135:Calcium-Binding Proteins / Q000097:blood*; D002850:Chromatography, Gel; D018260:Gelsolin; D008840:Microfilament Proteins / Q000097:blood*; D011485:Protein Binding; D011817:Rabbits; D013552:Swine
chemical_list: D000199:Actins; D002135:Calcium-Binding Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate