A chemical modification to make horseradish peroxidase soluble and active in benzene

  • Takahashi K
  • Nishimura H
  • Yoshimoto T
 et al. 
  • 5


    Mendeley users who have this article in their library.
  • 117


    Citations of this article.


Horseradish peroxidase was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine. The modified peroxidase, in which 60% of the amino groups were coupled with polyethylene glycol, had 70% of the enzymic activity in aqueous solution and was found to be soluble in benzene. Since the modified peroxidase in benzene had an absorption spectrum similar to that of unmodified peroxidase in aqueous solution, the prosthetic group, protohaemin IX, remained with the apoprotein even in benzene. The modified peroxidase in benzene had 21% of the enzymic activity relative to that of unmodified enzyme in aqueous solution. © 1984.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • K. Takahashi

  • H. Nishimura

  • T. Yoshimoto

  • Y. Saito

  • Y. Inada

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free