甲醇的微生物氧化。假单胞菌属M27醇脱氢酶的纯化及性质
The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27.
作者信息
Anthony C, Zatman L J
出版信息
Biochem J. 1967 Sep;104(3):953-9. doi: 10.1042/bj1040953.
Abstract
- A method for the purification of the nicotinamide nucleotide-independent alcohol dehydrogenase of Pseudomonas sp. M27 is described. 2. In the analytical ultracentrifuge, the purified enzyme shows a single major component of molecular weight 146000. 3. On electrophoresis in polyacrylamide gels between pH5.0 and 9.55, it shows only one protein band and the isoelectric point appears to be between pH7.0 and 8.0. 4. Spectrographic analysis indicates no significant metal content. 5. Amino acid analysis shows an unusually small number of cysteine/cystine residues per molecule as well as about 4.1% of glucosamine. 6. The role of ammonia as enzyme activator has been investigated.
摘要
- 本文描述了一种纯化假单胞菌属M27的烟酰胺核苷酸非依赖性乙醇脱氢酶的方法。2. 在分析超速离心机中，纯化后的酶显示出单一主要成分，分子量为146000。3. 在pH5.0至9.55的聚丙烯酰胺凝胶中进行电泳时，它仅显示一条蛋白带，等电点似乎在pH7.0至8.0之间。4. 光谱分析表明金属含量不显著。5. 氨基酸分析显示每个分子中半胱氨酸/胱氨酸残基的数量异常少，以及约4.1%的氨基葡萄糖。6. 对氨作为酶激活剂的作用进行了研究。
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