Leishmania tarentolae: purification and characterization of tubulin and its suitability for antileishmanial drug screening.

ABSTRACT: Previously, tubulin has been purified from Leishmania amazonensis and used to identify novel molecules with selective antimitotic activity. However, L. amazonensis is pathogenic and requires a relatively expensive medium for large-scale cultivation. Herein, the purification and characterization of tubulin from the non-pathogenic Leishmania tarentolae is reported, together with the sequence of alpha- and beta-tubulin from this organism. This protein was purified by sonication, diethylaminoethyl-Sepharose chromatography, and one assembly disassembly cycle in 1% overall recovery based on total cellular protein. Leishmania tarentolae tubulin was indistinguishable from the corresponding L. amazonensis protein in terms of binding affinity for dinitroaniline sulfanilamides and sensitivity to asse

SUBMITTER: Yakovich AJ 

PROVIDER: S-EPMC1986769 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature