Department of Biological Sciences, State University of New York, Binghamton, New York 13901.
Plant Physiol. 1976 Sep;58(3):248-52. doi: 10.1104/pp.58.3.248.
An l-cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus has been purified approximately 200-fold. The enzyme uses selenocysteine as substrate in the ATP-PPi exchange assay; other cysteine analogs were inactive. The molecular weight as determined by Sephadex G-200 column chromatography is about 61,000; sodium dodecyl sulfate and 8 m urea acrylamide gel electrophoresis indicate that the enzyme is a dimer consisting of two identical monomers of molecular weight 30,000. A method for the preparation of selenocysteine from selenocystine is described.
来自 Phaseolus aureus 的 l-半胱氨酰-tRNA 合成酶(EC 6.1.1.16)已被纯化约 200 倍。该酶在 ATP-PPi 交换测定中使用硒代半胱氨酸作为底物;其他半胱氨酸类似物没有活性。通过 Sephadex G-200 柱层析法测定的分子量约为 61,000;十二烷基硫酸钠和 8 m 尿素丙烯酰胺凝胶电泳表明,该酶是由分子量为 30,000 的两个相同单体组成的二聚体。描述了一种从硒代胱氨酸制备硒代半胱氨酸的方法。