| Autor: |
Makino, Nobuo, McMahill, Paul, Mason, Howard S., Moss, Thomas H. |
| Zdroj: |
Journal of Biological Chemistry; October 1974, Vol. 249 Issue: 19 p6062-6066, 5p |
| Abstrakt: |
Resting tryosinase was diamagnetic between 1.4 K and 200 K. Redox titration showed that it, but not apotyrosinase, contained a titrable group, E′0= +0.36 volt (pH 7.0), n= 2. Upon denaturation with acid under strictly anaerobic conditions, the EPR-detectable copper increased from less than 5% of the copper present to about 100%. It is concluded that the active site of the enzyme contains a pair of antiferromagnetically coupled Cu2+ions. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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