Dityrosine formation in calmodulin: cross-linking and polymerization catalyzed by Arthromyces peroxidase

Biochemistry
D A Malencik, S R Anderson

Abstract

We employ bovine brain calmodulin, a protein that is subject to photoactivated dityrosine formation [Malencik, D. A., & Anderson, S. R. (1987) Biochemistry 26, 695; (1994) Biochemistry 33, 13363], as a model for the development of an efficient enzyme-catalyzed protein cross-linking technique. Key steps in the elaboration of the procedure are (1) identification of a peroxidase, from Arthromyces ramosus, that catalyzes dityrosine production in proteins that are not acted on by other common peroxidases, (2) monitoring of the intrinsic fluorescence of dityrosine to determine optimum reaction conditions, achieved with calmodulin in solutions containing boric acid-sodium borate (concentration > or = 0.2 M), approximately pH 8.3, approximately 40 degrees C, and (3) quenching of the reaction with reduced glutathione. Arthromyces peroxidase is the only common peroxidase able to catalyze significant dityrosine production in calmodulin, through a reaction that is largely intermolecular. Gel filtration yields fractions (accounting for approximately 40% of the initial calmodulin) that represent differing mobility ranges in NaDodSO4 polyacrylamide gel electrophoresis and contain close to the maximum possible amounts of dityrosine. The variou...Continue Reading

References

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