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Studies of the enzyme laccase


Kanne, Robert M. (1983) Studies of the enzyme laccase. Master's thesis, California Institute of Technology. doi:10.7907/8yyp-a776.


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)
Subject Keywords:Chemistry
Degree Grantor:California Institute of Technology
Division:Chemistry and Chemical Engineering
Major Option:Chemistry
Thesis Availability:Public (worldwide access)
Research Advisor(s):
  • Gray, Harry B.
Thesis Committee:
  • Unknown, Unknown
Defense Date:27 May 1983
Record Number:CaltechTHESIS:04022010-090654360
Persistent URL:
Default Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:5678
Deposited By: Tony Diaz
Deposited On:16 Apr 2010 22:45
Last Modified:16 Apr 2021 22:14

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