Abstract
The inhibitory effect of S-100 on microtubule protein assembly is inversely related to the microtubule protein concentration and/or the temperature of assembly. Moreover, the S-100-induced decrease in the rate and extent of assembly is positively correlated with the length of the lag of assembly. When microtubule fragments are added to the microtubule protein solution, the S-100 effect is reduced but not abolished. These data suggest that S-100 interferes with both the nucleation and the elongation of microtubules. Since S-100 also inhibits the assembly of purified tubulin, S-100 is suggested to affect the microtubule assembly by interacting with and sequestering tubulin.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
