ニジマス肝臓のβ-ガラクトシダーゼに関する研究-1-精製および二・三の性質

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In an earlier paper1) dealing with the distribution of glycosidases in fish, it was shown that the β-galactosidase activity is found in every fish tissue. In this paper, the purification procedure of β-galactosidase from the rainbow trout liver and some properties of the enzyme were described. 1. The β-galactosidase was extracted from the liver of rainbow trout of which the average body weight was 150g. Two isozymes of β-galactosidase were isolated by the Sephadex column chromatography. The molecular weights of the isozymes estimated by the gel filtration were 340, 000 for β-galactosidase I and 170, 000 for β-galactosidase II. 2. The optimal pH range for both isozymes was 3.8-4.2, and the stable pH range was 4.5-6.5. 3. The activation energy calculated from the ARRHENIUS plots was about 13, 000 cal./mole for both isozymes. The thermostability of the enzyme I was predominant to that of the emzyme II. 4. There was no extreme difference between the Km values of o- and p-nitrophenyl-β-D-galactoside for both isozymes.
社団法人日本水産学会の論文