Ox. reagent for proteins

Scott B. Mulrooney ef075 at cleveland.Freenet.Edu
Fri Dec 16 00:59:38 EST 1994


You might want to check an article in the Dec. 10 1993
issue of Science by Derman et. al., p 1744. They used a
cytoplasmic version of alkaline phosphatase (which needs
oxidized disulfides to be enzymatically active) to look for
E. coli mutants that had this phosphatase active in the 
cytoplasm, rather than the usual inactive, disulfide reduced
form. They got many mutations, all of which mapped to the
gene for thioredoxin reductase (the enzyme I am working on).
Mutants lacking thioredoxin reductase resulted in a more
oxidized cytoplasmic environment. They sent us several of
their mutants, and if you want to try, I'm sure they will
send you some. Feel free to E-mail me if you have any further
questions.


Scott Mulrooney
Department of Biological Chemistry
University of Michigan
E-mail: mulrsb at umich.edu



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