Popov V O, Shumilin I A, Ustinnikova T B, Lamzin V S, Egorov Ts A
Bioorg Khim. 1990 Mar;16(3):324-35.
The primary structure of NAD-dependent formate dehydrogenase from methylotrophic bacterium Pseudomonas sp. 101 is determined. The enzyme is composed of two identical subunits, each comprising 393 amino acid residues, and has a molecular weight of 43.1 kD. To elucidate the protein's amino acid sequence, four types of digestion were used: cyanogen bromide cleavage at methionine residues, endoproteinase Lys-C digestion at lysine residues, endoproteinase Glu-C cleavage at glutamic acid residues, and tryptic digestion. The peptides obtained were purified to homogeneity and characterized.
确定了甲基营养型细菌假单胞菌属101中依赖烟酰胺腺嘌呤二核苷酸(NAD)的甲酸脱氢酶的一级结构。该酶由两个相同的亚基组成,每个亚基包含393个氨基酸残基,分子量为43.1千道尔顿。为了阐明该蛋白质的氨基酸序列,使用了四种消化方法:在甲硫氨酸残基处进行溴化氰裂解、在赖氨酸残基处进行内肽酶Lys-C消化、在谷氨酸残基处进行内肽酶Glu-C裂解以及胰蛋白酶消化。获得的肽段被纯化至均一性并进行了表征。