Some Physico-Chemical Properties of a Stable Albumin Free Radical.
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Crystalline bovine serum albumin was converted to a stable free radical form by reaction with nitrosyl disulfonate in alkaline solution. The purified free radical protein showed a characteristic single EPR peak at G2, both in aqueous solution at room temperature and in the solid state at liquid nitrogen temperatures. The free radical signal was intensified by visible light. The free radical state of the protein was characterized by unique changes in the visible, ultraviolet, and fluorescence spectra. Attempts to quantitate the number of free radical sites on the albumin by titration with dithiothreitol indicated that the number of radical sites correlated with the number of tyrosine and tryptophan residues in the molecule. Author
- Physical Chemistry