Veronese F M, Boccu E, Conventi L
Biochim Biophys Acta. 1975 Feb 19;377(2):217-28. doi: 10.1016/0005-2744(75)90304-6.
When Escherichia coli was grown in a minimum medium with glucose as sole carbon source and a proper level of ammonia, NADP+ specific glutamate dehydrogenase (L-glutamate: NADP+ oxidoreductase (deaminating), ED 1.4.1.4) was induced. The enzyme was solubilized by French press treatment and purified to homogeneity by (NH4)2SO4 fractionation, heat treatment followed by DEAE-cellulose, hydroxylapatite and Bio-Gel chromatography with an overall yield of 30%. The enzyme proved to be heat stable and relatively resistant to protein denaturants. The optimum of enzymic activity for the reductive amination is at pH 8 and at pH 9 for the oxidative deamination. The activity is affected by adenine nucleotides. The molecular weight (about 250 000 for the native form and 46 000 for the inactive subunit) and amino acid composition, suggest strict similarities with the NADP+ enzyme from fungal origin.
当大肠杆菌在以葡萄糖作为唯一碳源且含有适量氨的基本培养基中生长时，会诱导产生NADP⁺特异性谷氨酸脱氢酶（L-谷氨酸：NADP⁺氧化还原酶（脱氨基），EC 1.4.1.4）。该酶通过法国压榨机处理进行溶解，并通过硫酸铵分级分离、热处理，随后进行DEAE-纤维素、羟基磷灰石和Bio-Gel柱层析纯化至均一，总产率为30%。该酶被证明具有热稳定性且相对抗蛋白质变性剂。还原胺化的酶活性最佳pH值为8，氧化脱氨基的最佳pH值为9。其活性受腺嘌呤核苷酸影响。分子量（天然形式约为250000，无活性亚基为46000）和氨基酸组成表明，与真菌来源的NADP⁺酶有严格的相似性。
