Abstract
An attempt was made to purify the thiaminase II from the culture broth of Bacillus aneurinolyticus Kimura et Aoyama. A crude enzyme preparation was obtained by an osmotic concentration method as a precipitate at 25-60% saturation of ammonium sulfate. The crude enzyme preparation was dissolved in phosphate buffer (pH 7.4) and fractionated with several ion exchange resins. The enzymic activity of a protein solution which passed throuth the cation exchanger, such as Amberlite IR-120 or IRC-50 was decreased, while that of a solution which passed through the anion exchanger, such as Amberlite IRA-400 or IR-4B was considerably increased. Form the above results and the examination of the absorption spectrum of protein solutions, it was supposed that the crude enzyme preparation contained an enzyme-protein, metallic ions and an acidic substance having an absorption maximum at 250 mμ.
