Ramaley R F, Vasantha N
J Biol Chem. 1983 Oct 25;258(20):12558-65.
Bacillus subtilis glucose dehydrogenase (EC 1.1.1.47) has been purified from sporulating cell extract to apparent homogeneity (as determined by polyacrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and isoelectric focusing). The enzyme purified as a single molecular species with no evidence for a multiple form of the enzyme. The B. subtilis glucose dehydrogenase has an apparent isoelectric point of 4.7-4.8 and an apparent Mr = 126,000 and is comprised of four subunits of Mr = 31,500 each. The glucose 2-deoxyglucose and glucosamine substrate specificity of the enzyme is similar to the substrate specificity for B. subtilis spore germination, suggesting that the spore glucose dehydrogenase may play some role in spore germination. The B. subtilis glucose dehydrogenase is extremely dependent on the presence of glycerol or other hydrophobic bond-stabilizing agents (or NAD) for retention of enzymatic activity, and the presence of glycerol (20% w/v) in the extraction and purification buffers was absolutely necessary for the successful purification of this enzyme.
枯草芽孢杆菌葡萄糖脱氢酶（EC 1.1.1.47）已从芽孢形成细胞提取物中纯化至表观均一（通过聚丙烯酰胺凝胶电泳、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和等电聚焦测定）。该酶作为单一分子形式纯化，没有证据表明存在多种形式的酶。枯草芽孢杆菌葡萄糖脱氢酶的表观等电点为4.7 - 4.8，表观Mr = 126,000，由四个Mr = 31,500的亚基组成。该酶对葡萄糖、2-脱氧葡萄糖和氨基葡萄糖的底物特异性与枯草芽孢杆菌孢子萌发的底物特异性相似，这表明孢子葡萄糖脱氢酶可能在孢子萌发中发挥某种作用。枯草芽孢杆菌葡萄糖脱氢酶极其依赖甘油或其他疏水键稳定剂（或NAD）的存在来保持酶活性，并且在提取和纯化缓冲液中存在甘油（20% w/v）对于成功纯化该酶绝对必要。
