Keller B, Keller E, Lingens F
Biol Chem Hoppe Seyler. 1985 Nov;366(11):1063-6. doi: 10.1515/bchm3.1985.366.2.1063.
Arogenate dehydrogenase, the terminal enzyme of tyrosine biosynthesis in Streptomyces phaeochromogenes, was purified to homogeneity by a five-step procedure. The enzyme is a dimer of Mr 57 600 as determined by dodecyl sulfate polyacrylamide gel electrophoresis after cross-linking of the monomers, or of 66 300 as found by gel permeation chromatography, and consists of two identical subunits of Mr 28 100. The pI of the enzyme is 4.45, and the Km values are 0.105mM for arogenate and 0.01 mM for NAD.
在产色链霉菌中，酪氨酸生物合成的末端酶——对羟基苯丙酮酸双加氧酶，通过五步纯化程序被纯化至同质。经单体交联后，通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳测定，该酶为分子量57600的二聚体；通过凝胶渗透色谱法测定，其分子量为66300，由两个分子量为28100的相同亚基组成。该酶的等电点为4.45，对羟基苯丙酮酸的米氏常数为0.105 mM，烟酰胺腺嘌呤二核苷酸的米氏常数为0.01 mM。
