THE PURIFICATION OF THIAMINASE I PRODUCED BY BACILLUS THIAMINOLYTICUS

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概要

• 論文の詳細を見る

• 1. Purification of the thiaminase I produced by B. thiaminolyticus Matsukawa et Misawa has been described. By applying the 70% ammonium sulfate fraction of crude thiaminase I to chromatographic fractionation using an ion exchange resin, Duolite A2, and zone electrophoresis, an enzyme preparation having 200 times as much specific activity as that of the original crude enzyme was obtained. Ultracentrifugal analysis indicated that the preparation contained a single component and was free from any organic bases. The purified thiaminase alone does not show any thiaminase activity, but its activity appears in the presence of an organic base (pyridine) leading to the formation of heteropyrithiamine.2. Km for thiamine and pyridine of the purified enzyme were 0.9×10-3 and 1.0×10-3M at pH 6.5 and 30°, respectively, according to Lineweaver and Burk's method. Vmax was 190mg/min/mg protein-N, expressed as the amount of thiamine decomposed.3. The sedimentation constant and other observations suggest a molecular weight of approximately 40, 000.4. According to the results of inhibition experiments, the enzyme is considered to be an SH-enzyme.

• 日本ビタミン学会の論文

著者

• Murata Kiku

  Nutrition Laboratory, Faculty of the Science of Living, Osaka City University

• Ebata J.

  Nutrition Laboratory, School of Science of Living, Osaka City University

関連論文

• REACTIVATION MECHANISMS OF THIAMINE WITH TERMOSTABLE FACTORS
• THE PURIFICATION OF THIAMINASE I PRODUCED BY BACILLUS THIAMINOLYTICUS

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