ausblenden:
Schlagwörter:
Triethyllead chloride, Microtubule assembly, Sulfhydryl group, Disulfide, Thiol reagents, DTNB, 5,5'-dithiobis(2-nitrobenzoic acid), DNPSSG, 2,4-dinitrophenylglutathionyl disulfide, Et3Pb+, triethyllead ion, MAPs, microtubule-associated proteins
Zusammenfassung:
Triethyllead ion (Et3Pb+) was found to interact with 2 out of 18 thiol groups present in tubulin dimers. Specificity of the interaction was shown by the high affinity of Et3Pb+ to tubulin, by the fact that the 16 residual thiol groups in tubulin remained unaffected, and by the observation that other proteins with exposed thiol groups, e.g., actin, did not react with Et3Pb+. After complexation of the two thiol groups, tubulin in vitro had lost its capability for microtubule assembly. Likewise, polymerized tubulin disassembled on addition of the lead compound.
