作者: J.R. Zabrecky , R.D. Cole
DOI: 10.1016/S0021-9258(19)70230-0
关键词: GTP' 、 A-site 、 Ion exchange 、 Tubulin 、 Nucleotide 、 Bovine brain 、 Stereochemistry 、 Microtubule 、 Chemistry
摘要: Abstract Aggregates of double-walled rings (46 nm diameter) were formed upon warming (37 degrees C) ion exchange purified bovine brain tubulin (1.5 to 2.0 mg/ml) in the presence 1.0 mM ATP and 5.0 Mg2+. The formation aggregated was blocked by GDP (1.0 mM), but when GTP mM) added subsequently, block overcome. Warming simultaneously produced a mixture microtubules rings. preparations used demonstrated be devoid transphosphorylase, it is therefore clear that action induction not mediated transphosphorylation. These results are consistent with an interaction nucleotide at site distinct from previously described N- E-sites.