UNSPECIFIC ARGININE KINASE OF MOLECULAR WEIGHT 150000 - PURIFICATION AND PROPERTIES
UNSPECIFIC ARGININE KINASE OF MOLECULAR WEIGHT 150000 - PURIFICATION AND PROPERTIES
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DOI：
10.1111/j.1432-1033.1971.tb01453.x
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发表时间：
1971-01-01
期刊：
影响因子：
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通讯作者：
THOAI, NV
中科院分区：
文献类型：
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作者：
ROBIN, Y;KLOTZ, C;THOAI, NV
精氨酸激酶已从海洋多毛类环节动物Sabella pavonina的体壁肌肉中纯化出来。制备的样品在分析超离心和聚丙烯酰胺凝胶圆盘电泳中均质。该酶是不稳定的，即使在保护剂的存在下，其比活性也会迅速降低。天然酶的分子量为150000 ± 5000，沉降系数为20，b = 7.5。wt 43000）和裸方格星虫（Sipunculusnudusmuscle.野生型83000），来自沙伯菌的磷酸激酶对精氨酸没有严格的特异性。该酶没有显示出光学异构体特异性，并且对许多l-精氨酸类似物具有轻微活性，其胍和羧基的完整性对其活性是必不可少的。部分同位素交换和动力学研究表明，该酶的反应机制与海水甲壳类动物肌肉精氨酸激酶的反应机制有些不同，而与其他磷酸原磷酸激酶的反应机制更相似。
Arginine kinase has been purified from body‐wall muscle of a marine polychaetous annelid,Sabella pavonina.The preparation is homogeneous to analytical ultracentrifugation and disc electrophoresis on polyacrylamide gel. The enzyme is labile and undergoes a rapid decrease of its specific activity, even in the presence of protecting agents. The molecular weight of the native enzyme is 150 000 ± 5000, the sedimentation coefficients°20,bbeing found to be equal to 7.5.Unlike the enzyme from lobster muscle (mol. wt ≃ 43000) and that fromSipunculus nudusmuscle (mol. wt ≃ 83000), the phosphokinase fromSabella pavoninamuscle is not strictly specific towardsl‐arginine. The enzyme shows no optical isomer specificity and is slightly active on a number of analogues ofl‐arginine, the integrity of the guanidine and carboxylic groups of which is indispensable to their activity. The enzyme is strictly specific for the nucleotidic substrate ATP.Partial isotopic exchange and kinetic studies suggest that the reaction mechanism is somewhat different from that described for sea‐water crustacean muscle arginine kinase and more similar to that reported for other phosphagen phosphokinases.