Kanne, Robert M. (1983) Studies of the enzyme laccase. Master's thesis, California Institute of Technology. http://resolver.caltech.edu/CaltechTHESIS:04022010-090654360
Rhus Vernicifera laccase was purified to an A_(280)/A_(614) ratio of 15.2. A procedure was then used to selectively remove the Type 2 copper and 70% of it was removed as judged by EPR. The treated enzyme showed decreased absorbance in the 330 nm, region, which is associated with the Type 3 site, The blue color was observed to reversibly bleach on occasion, apparently due to autoreduction of the Type 1 copper. The fluorescence of the Type 2 depleted laccase was increased 60% over that of the native protein. Since fluorescence quenching is often associated with binding of a metal to a protein site, fluorescence was used to monitor the attempted substitution of cobalt and nickel into the Type 2 site, There is some evidence that cobalt can occupy the Type 2 site.
|Item Type:||Thesis (Master's thesis)|
|Degree Grantor:||California Institute of Technology|
|Division:||Chemistry and Chemical Engineering|
|Thesis Availability:||Restricted to Caltech community only|
|Defense Date:||27 May 1983|
|Default Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||16 Apr 2010 22:45|
|Last Modified:||26 Dec 2012 03:24|
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