魚類におけるヒスチジン代謝-III : マサバ筋肉中のヒスチジンデアミナーゼの精製と二,三の性質

概要

論文の詳細を見る
1. A procedure for obtaining a partially purified preparation of histidine deaminase from mackerel muscle was developed and some properties of the enzyme were examined. 2. The deaminase was purified from mackerel muscle about 380-fold using a method of fractionation employing ammonium sulfate, heat-treatment, DEAE-Sephadex chromatography, hydroxylapatite chromatography and Sephadex G-200 gel-filtration. 3. The enzyme was relatively stable at the temperature below 55°C, at the alkaline condition. 4. The pH optimum of the enzyme was found at 9.0. 5. Metals, with the exception of Zn and pCMB showed slight or strong inhibitory effects on the enzyme action, but EDTA did not cause an inhibition. SH compounds did not activate the enzyme reaction, however, the pCMB-inactivation was recovered by the addition of cysteine.