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Spectral studies of human erythrocyte catalase ec 1.11.1.6


, : Spectral studies of human erythrocyte catalase ec 1.11.1.6. Canadian Journal of Biochemistry 57(4): 321-329

The optical absorption and circular dichroic [CD] spectra of human erythrocyte catalase (EC 1.11.1.6) and its cyanide, azide and fluoride derivatives over the wavelength range of 210-700 nm are reported. Treatment with acid or alkaline solutions causes spectral changes which are due to dissociation of the enzyme into subunits and removal of the heme group from the protein. The fractions of the protein structure present as .alpha. helix, .beta. pleated sheet and unordered structure were estimated from the CD spectrum in the far-UV region. The CD spectra indicate that the protein conformation does not change appreciably after cyanide binding. The EPR spectroscopy of the native enzyme and its cyanide complex is reported. The spectral results are compared with catalase obtained from other mammalian and bacterial sources.

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