Hirel B, McNally S F, Gadal P, Sumar N, Stewart G R
Eur J Biochem. 1984 Jan 2;138(1):63-6. doi: 10.1111/j.1432-1033.1984.tb07881.x.
Cytosolic glutamine synthetase (GS1) was purified to homogeneity from etiolated barley leaves by DEAE-Sephacel and hydroxyapatite chromatography, gel filtration and polyacrylamide gel electrophoresis. Specific antibodies against the purified protein were raised by the immunization of rabbits. Immunoprecipitation experiments demonstrated that cytosolic glutamine synthetases isolated from the leaves of different plant species were very similar proteins. Good recognition of other cytosolic glutamine synthetases from roots, root nodular tissue and seeds by barley GS1 antibodies was obtained, suggesting that they too are all quite similar proteins. In contrast, chloroplast glutamine synthetase (GS2) was considered to be a different protein in view of its low level of recognition by barley GS1 antibodies.
通过DEAE-葡聚糖凝胶和羟基磷灰石色谱、凝胶过滤及聚丙烯酰胺凝胶电泳,从黄化大麦叶片中纯化出了均一的胞质谷氨酰胺合成酶(GS1)。通过免疫兔子制备了针对纯化蛋白的特异性抗体。免疫沉淀实验表明,从不同植物物种叶片中分离得到的胞质谷氨酰胺合成酶是非常相似的蛋白质。大麦GS1抗体能够很好地识别来自根、根瘤组织和种子的其他胞质谷氨酰胺合成酶,这表明它们也是非常相似的蛋白质。相比之下,鉴于大麦GS1抗体对叶绿体谷氨酰胺合成酶(GS2)的识别水平较低,它被认为是一种不同的蛋白质。