Brolin S E, Borglund E, Agren A
J Biochem Biophys Methods. 1979 Jul;1(3):163-9. doi: 10.1016/0165-022x(79)90035-6.
A new rapid photokinetic method is described for determining the activity of adenylate kinase (ATP:AMP phosphotranspherase, EC 2.7.4.3) in 0.1--5.0 micrograms of freeze-dried tissue. This represents a weight range far below that obtainable by fine-needle biopsy. The reaction 2 ADP in equilibrium with AMP + ATP was employed and the ATP formed assayed with firefly luciferase as light yielder. The light emission was recorded on a multi-channel scaler. The adenylate kinase activities found in tissues of mice were in the same range as previously described in a study using fluorometric microassay.
本文描述了一种新的快速光动力学方法，用于测定0.1至5.0微克冻干组织中腺苷酸激酶（ATP：AMP磷酸转移酶，EC 2.7.4.3）的活性。这一重量范围远低于细针穿刺活检所能获得的重量范围。采用2 ADP与AMP + ATP平衡的反应，并以萤火虫荧光素酶作为发光体来测定生成的ATP。发光情况通过多道定标器记录。在小鼠组织中发现的腺苷酸激酶活性与之前使用荧光微量测定法的研究中所描述的范围相同。
