鶏血漿中F-GOTの酵素作用の性質について : II. F-GOT反応におけるpHの影響

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The pH depenclence of F-GOT activity wzas stuclned oxer a pH range from6.0 to 9.0. Phosphate and Tris-HCI buffers were uscd as solvents for substrate, since the3?have a significant effect on transatninatiozt reaction. TIIC restzlts obtained are summarizedas follows.1. XVhen a pH-activity CUTXC was drawn, it suggested a possibility tltat phosphate tonmight have acted as a catalyst, and sodium and potassiurn tons as inhibitors. XVithinta pH range from 6.0 to 7.8, tlte op[irrxuna pH xalues were 7.0 and 7.2.2. The Tris-HCI buffer was less actixe than tlae phospltate one at both optimum pHvalues.A most striking feature was that although the curve obtained with the Tris-IICI buf[ex-was composed of three curves which presented a peak at an alkaline pH value withina range of 7.0-7.2 attd 8.0-8.2, and at pH 8.6, respectively, 110 liberation of pyridoxal5-phosphate from the denatttred enzyme was recognized.Apparently, that cturve was characteristic in showing tlae fccllowing significance. Tl?emaximal velocity and the Michaelis constant for alpha-ketoglutarate were not dependentupon pH value within a pH range from 7.0 to 9.0. The enzyme was stable, and the sub-strate does not ionize throughout this pH range.These results suggest that the variation in activity may l?ave been induced by theionization of some groups contained in the enzyme. They also indicate that the methodof assay used in this experiment was satisfactory even at a pH value exceeding 8.5.
社団法人日本獣医学会の論文
1976-04-25

鶏血漿中F-GOTの酵素作用の性質について : II. F-GOT反応におけるpHの影響

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