Jump to content

  • Log in with Facebook Log in with Twitter Log in with Windows Live Log In with Google      Sign In   
  • Create Account

Submit your paper to J Biol Methods today!
- - - - -

Enzyme kinetics

  • Please log in to reply
1 reply to this topic

#1 moljul



  • Active Members
  • PipPipPipPipPipPipPipPipPipPip
  • 142 posts

Posted 23 February 2009 - 12:19 AM

im not familiar with this stuff, therefore i hope to get some suggestions and recommendations for the solution of my problem:

im working with bortezomib which is a selective and reversible inhibitor of the chymotryptic activity of the proteasome
i inject mice with this inhibitor, and have now to measure the inhibitory action of this compound in vivo.
therefore i have to isolate proteasomes and check for chymotryptic activity in the lysates.

my question now is a general one: when i isolate proteasomes with a special protocol to obtain high purified proteasomes, how will i know that acitivty was inhibited somehow?
the reversible inhibitor will not permanently bound to my proteasomes!

how can i really measure inhibitory activity of tissue samples???

thanks in advance

#2 Dr Teeth

Dr Teeth


  • Active Members
  • PipPipPipPipPipPipPipPipPipPip
  • 221 posts

Posted 25 February 2009 - 06:52 AM

Can you examine the expression of a subset of proteins targeted by the proteasome? In this case, you could examine the percent remaining for each protein or the amount of ubiquitinated protein compared to the un-inhibited proteasome controls where protein expression of these targets would be low due to degradation?

Science is simply common sense at its best that is rigidly accurate in observation and merciless to fallacy in logic.
Thomas Henry Huxley

Home - About - Terms of Service - Privacy - Contact Us

©1999-2013 Protocol Online, All rights reserved.