Protein phosphatase (PP) 2A1, a trimer composed of A-, B-and C-subunits in the PP2A family, has been regarded as a principal form localizing at microtubules (MT), but PP2A2, the dimer of A-and C-subunits, has not. Substantiating the claim, the present work shows that the PP2A1 but not PP2A2, both isolated from bovine extract, largely associated with the purified preparation of MT. Furthermore, PP2A1 was found to bind purified tubulin polymerized by taxol. The presence of MT associated proteins with purified tubulin hardly affected the binding of PP2A1 to the tubulin. In addition, PP2A1 activity towards glycogen phosphorylase, a probably unphysiological but good substrate, was similarly inhibited by MT proteins and purified tubulin, which accounts for 85 % of MT proteins, with their IC &! of about 0n15 mg\ml. In contrast, the inhibition of PP2A2