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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Boulton C A, Large P J

Biochim Biophys Acta. 1979 Sep 12;570(1):22-30. doi: 10.1016/0005-2744(79)90197-9.

The primary-amine dehydrogenase of Pseudomonas AM1 (primary amine:(acceptor) oxidoreductase (deaminating), EC 1.4.99.-) was purified by an improved method and covalently attached to cyanogen bromide-activated Sepharose 4B. The immobilized enzyme showed very little change in its sensitivity to heat and to inhibition by semicarbazide as compared with the soluble enzyme, but had enhanced stability at 0 degrees C. The pH optimum of the immobilized enzyme remained unchanged at pH 7.4. 2. A new type of spectrophotometric assay is described in which sedimentation of the immobilized enzyme in the cuvette is prevented by increasing the viscosity by the presence of 10% (w/w) polyethylene glycol (M1 20 000). Detailed kinetic analysis using this assay showed only insignificant differences in the Km values for n-butylamine and phenazine methosulphate between the soluble and Agarose-bound enzymes. The results are compared with those for other oxidoreductase enzymes immobilized on Sepharose.

通过改进方法纯化了假单胞菌AM1的伯胺脱氢酶（伯胺：（受体）氧化还原酶（脱氨基），EC 1.4.99.-），并将其共价连接到溴化氰活化的琼脂糖4B上。与可溶性酶相比，固定化酶对热的敏感性和对氨基脲抑制的敏感性变化很小，但在0℃时稳定性增强。固定化酶的最适pH在pH 7.4时保持不变。2. 描述了一种新型的分光光度法测定方法，其中通过存在10%（w/w）聚乙二醇（M1 20 000）增加粘度来防止固定化酶在比色皿中沉淀。使用该测定方法的详细动力学分析表明，可溶性酶和琼脂糖结合酶之间正丁胺和吩嗪硫酸甲酯的Km值仅存在微不足道的差异。将结果与固定在琼脂糖上的其他氧化还原酶的结果进行了比较。

Boulton C A, Large P J

Biochim Biophys Acta. 1979 Sep 12;570(1):22-30. doi: 10.1016/0005-2744(79)90197-9.

The primary-amine dehydrogenase of Pseudomonas AM1 (primary amine:(acceptor) oxidoreductase (deaminating), EC 1.4.99.-) was purified by an improved method and covalently attached to cyanogen bromide-activated Sepharose 4B. The immobilized enzyme showed very little change in its sensitivity to heat and to inhibition by semicarbazide as compared with the soluble enzyme, but had enhanced stability at 0 degrees C. The pH optimum of the immobilized enzyme remained unchanged at pH 7.4. 2. A new type of spectrophotometric assay is described in which sedimentation of the immobilized enzyme in the cuvette is prevented by increasing the viscosity by the presence of 10% (w/w) polyethylene glycol (M1 20 000). Detailed kinetic analysis using this assay showed only insignificant differences in the Km values for n-butylamine and phenazine methosulphate between the soluble and Agarose-bound enzymes. The results are compared with those for other oxidoreductase enzymes immobilized on Sepharose.

通过改进方法纯化了假单胞菌AM1的伯胺脱氢酶（伯胺：（受体）氧化还原酶（脱氨基），EC 1.4.99.-），并将其共价连接到溴化氰活化的琼脂糖4B上。与可溶性酶相比，固定化酶对热的敏感性和对氨基脲抑制的敏感性变化很小，但在0℃时稳定性增强。固定化酶的最适pH在pH 7.4时保持不变。2. 描述了一种新型的分光光度法测定方法，其中通过存在10%（w/w）聚乙二醇（M1 20 000）增加粘度来防止固定化酶在比色皿中沉淀。使用该测定方法的详细动力学分析表明，可溶性酶和琼脂糖结合酶之间正丁胺和吩嗪硫酸甲酯的Km值仅存在微不足道的差异。将结果与固定在琼脂糖上的其他氧化还原酶的结果进行了比较。