Lambeir_1983_Arch.Biochem.Biophys_220_549

Reference

Title : A kinetic and spectral study of the alkaline transitions of chloroperoxidase - Lambeir_1983_Arch.Biochem.Biophys_220_549
Author(s) : Lambeir AM , Dunford HB
Ref : Archives of Biochemistry & Biophysics , 220 :549 , 1983
Abstract :

The optical spectrum of chloroperoxidase in the near ultraviolet and visible region was studied from pH 6 to 12. Chloroperoxidase undergoes a first transition which is irreversible at pH 7 and a second transition near pH 11. The second transition is reversible provided the incubation period above pH 11 is kept as short as possible. The spectral properties of the intermediates were studied in the Soret region by means of a rapid scan apparatus. The rates of the transitions were measured in a stopped-flow apparatus. The pH dependence of both the spectra and the rate constants indicate that at least three ionizations are involved in the first alkaline transition.

PubMedSearch : Lambeir_1983_Arch.Biochem.Biophys_220_549
PubMedID: 6824339

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Citations formats

Lambeir AM, Dunford HB (1983)
A kinetic and spectral study of the alkaline transitions of chloroperoxidase
Archives of Biochemistry & Biophysics 220 :549

Lambeir AM, Dunford HB (1983)
Archives of Biochemistry & Biophysics 220 :549