title: Purification and characterization of an inhibitor protein with cytochalasin-like activity from bovine adrenal medulla.
abstract: A protein preparation with cytochalasin-like activity has been obtained from bovine adrenal medulla. Analysis by electrophoresis in SDS-polyacrylamide gel and chromatography in a Sephacryl S-200 column indicated that the inhibitor activity coincided with a 90 000 dalton polypeptide. The inhibitor decreased high-affinity binding of [3H]cytochalasin B to actin nuclei, apparently by competing with the drug for the same binding site. At substoichometric levels, the inhibitor had a potent effect on actin filament elongation and on actin-dependent gelation of cell extracts in vitro. These results suggest that the inhibitor may be involved in the control of actin filament assembly and interaction in the adrenal medulla.
mesh_terms: D000199:Actins / Q000378:metabolism; D000313:Adrenal Medulla / Q000032:analysis*; D000818:Animals; D002417:Cattle; D003571:Cytochalasin B / Q000378:metabolism; D003572:Cytochalasins / Q000302:isolation & purification*; D003599:Cytoskeleton / Q000378:metabolism; D008970:Molecular Weight; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects
chemical_list: D000199:Actins; D003572:Cytochalasins; D003571:Cytochalasin B