Thiem N V, Lacombe G, Thoai N V
Biochim Biophys Acta. 1975 Jan 23;377(1):95-102. doi: 10.1016/0005-2744(75)90290-9.
Solen ensisensis muscle arginine kinase (ATP : L-arginine phosphotransferase, EC 2.7.3.3) was isolated in an homogeneous state. Its molecular weight was found to be about 80 000. The properties of this enzyme were compared with those of arginine kinase from Sipunculus nudus, an enzyme which also has a molecular weight of about 80 000. Both enzymes have several reactive thiol groups (8 thiol groups in the Solen kinase and 12 in the Sipunculus enzyme were titrateable with 5,5'-dithio-bis-(2-nitrobenzoic) acid and histidine residues (both enzymes have 6 reactive histidine residues). These kinases were, therefore, highly susceptible to oxidation. Both enzymes show the same pH optimum and absolute specificity towards the guanidine substrate, L-arginine. The reaction kinetics of both enzymes are of the sequential type. In the presence of alpha-aminoacids of Mg2+-ADP, similar spectral effects were obtained. The enzymes differ in their enzymic activities and in their rate of recovery following urea denaturation. The most important difference that appeared to be a special feature of the Sipunculus enzyme is that the spectrum of the Mg2+-ADP-enzyme complex is strongly intensified by L-arginine.
中国绿螂肌肉精氨酸激酶（ATP：L - 精氨酸磷酸转移酶，EC 2.7.3.3）以均一状态分离得到。其分子量约为80000。将该酶的性质与裸沙蚕精氨酸激酶的性质进行了比较，后者分子量也约为80000。两种酶都有几个反应性巯基（中国绿螂激酶中有8个巯基，裸沙蚕酶中有12个巯基可用5,5'-二硫代双（2 - 硝基苯甲酸）滴定）以及组氨酸残基（两种酶都有6个反应性组氨酸残基）。因此，这些激酶极易被氧化。两种酶都表现出相同的最适pH值以及对胍底物L - 精氨酸具有绝对特异性。两种酶的反应动力学均为顺序型。在存在α - 氨基酸的Mg2 + - ADP时，获得了相似的光谱效应。两种酶在酶活性以及尿素变性后的恢复速率方面存在差异。裸沙蚕酶似乎具有的一个特殊特征是，L - 精氨酸会强烈增强Mg2 + - ADP - 酶复合物的光谱。
