Onoagbe I O, Dickson A J
Comp Biochem Physiol B. 1987;86(1):179-83. doi: 10.1016/0305-0491(87)90194-5.
Tyrosine aminotransferase has been purified from chicken liver to homogeneity by a 5-step procedure. The resultant enzyme preparation has a specific activity (256 units activity/mg protein) comparable to results published for the enzyme purified from rat liver and represented an overall recovery of 35-40%. In terms of structure (native and subunit molecular weights, immunological reactivity, and kinetic parameters) (apparent Michaelis constants for L-tyrosine and 2-oxoglutarate, oxoacid specificity, pH optimum) the purified enzyme from chicken liver exhibits remarkable similarities to tyrosine amino-transferase from rat liver.
通过五步程序从鸡肝中纯化出了均一的酪氨酸转氨酶。所得的酶制剂比活性（256单位活性/毫克蛋白质）与从大鼠肝脏中纯化该酶所发表的结果相当，总回收率为35 - 40%。就结构而言（天然和亚基分子量、免疫反应性和动力学参数）（L - 酪氨酸和2 - 氧代戊二酸的表观米氏常数、氧代酸特异性、最适pH值），从鸡肝中纯化的酶与大鼠肝脏中的酪氨酸转氨酶表现出显著的相似性。
