The action of cytochalasin A on the in vitro polymerization of brain tubulin and muscle G-actin.
The presence of cytochalasin A inhibits the self-assembly of beef brain tubulin and rabbit muscle G-actin in vitro and also decreases the colchicine binding of tubulin. Prior reaction of cytochalasin A with 2-mercaptoethanol destroys its inhibitory effects. It is shown that cytochalasin A exerts its actions by reacting with sulfhydryl groups, possibly causing irreversible structural changes in the proteins. Cytochalasin B does not affect the tubulin assembly reaction.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001921:Brain; D002417:Cattle; D003078:Colchicine / Q000378:metabolism; D003572:Cytochalasins / Q000494:pharmacology*; D006023:Glycoproteins / Q000378:metabolism*; D008623:Mercaptoethanol / Q000494:pharmacology; D009132:Muscles; D011108:Polymers; D011487:Protein Conformation / Q000187:drug effects; D011817:Rabbits; D014404:Tubulin / Q000378:metabolism*
D000199:Actins; D003572:Cytochalasins; D006023:Glycoproteins; D011108:Polymers; D014404:Tubulin; D008623:Mercaptoethanol; D003078:Colchicine