Hydantoin drugs inhibit polymerization of pure microtubular protein.
5,5-Diphenylhydantoin or 5-(4-hydroxyphenyl)-5-phenylhydantoin, 3.6 X 10(-4) M, inhibited polymerization of purified pig brain tubulin 50% as measured by viscosometric assay and estimation of tubulin length by electron microscopy. 5,5-Diphenylhydantoin did not bind to the low molecular weight fraction of tubulin or to guanosinetriphosphate; it displaced colchicine weakly from its binding site. 5,5-Diphenylhydantoin did not depolymerize established microtubules, indicating that it differs from colchicine in site and mode of action.
D000818:Animals; D002498:Centrifugation; D003864:Depression, Chemical; D006023:Glycoproteins / Q000378:metabolism*; D006827:Hydantoins / Q000494:pharmacology*; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism; D010672:Phenytoin / Q000378:metabolism; D011108:Polymers / Q000378:metabolism; D011485:Protein Binding; D012265:Ribonucleotides / Q000378:metabolism; D013552:Swine; D014404:Tubulin / Q000378:metabolism*; D014783:Viscosity
D006023:Glycoproteins; D006827:Hydantoins; D011108:Polymers; D012265:Ribonucleotides; D014404:Tubulin; D010672:Phenytoin