Matsumoto T, Tobari J
J Biochem. 1978 Aug;84(2):461-5. doi: 10.1093/oxfordjournals.jbchem.a132147.
Methylamine dehydrogenase (MW: 105,000) of Pseudomonas sp. J was treated with a bifunctional cross-linking reagent, dimethyl suberimidate. Cross-linked proteins having different molecular -eights of 53,000, 64,000, 80,000, 93,000, and 103,000 were found in addition to 13,000 (light subunit) and 40,000 (heavy subunit) by SDS polyacrylamide gel electrophoresis. Isolated light and heavy subunits were separately treated with the reagent. The product having a molecular weight of 80,000 was found to be a major cross-linked protein for the heavy subunit but no product was found for the light subunit. A similar electrophoretic pattern was also obtained for the reconstituted enzyme from the subunits of Pseudomonas sp. J and for methylamine dehydrogenase of Pseudomonas AM1. These results suggest that methylamine dehydrogenases obtained from these two bacteria are both the alpha2beta2-type subunit enzyme and have a geometrically analogous subunit structure.
对假单胞菌属J菌株的甲胺脱氢酶（分子量：105,000）用双功能交联剂辛二亚氨酸二甲酯进行处理。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳发现，除了13,000（轻亚基）和40,000（重亚基）外，还存在分子量分别为53,000、64,000、80,000、93,000和103,000的交联蛋白。将分离得到的轻亚基和重亚基分别用该试剂处理。发现分子量为80,000的产物是重亚基的主要交联蛋白，但未发现轻亚基有产物。对来自假单胞菌属J菌株亚基的重组酶以及假单胞菌AM1的甲胺脱氢酶也得到了类似的电泳图谱。这些结果表明，从这两种细菌中获得的甲胺脱氢酶均为α2β2型亚基酶，且具有几何结构类似的亚基结构。
