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 |
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