Abstract
Treatment of flavocytochrome b 2 with 3 M urea produces a reversible inactivation of the enzyme. Higher urea concentrations inactivate it irreversibly. Chromatography on a calcium triphosphate column of the urea-treated enzyme shows that the enzyme molecule is dissociated into three fragments: a polynucleotide, a flavine fraction, and a hemoprotein similar to that obtained by Yamashita et al. Some properties of these fractions have been studied and the nature of the bonds between them has been discussed.
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