Bruneau J M, Worrell A C, Cambou B, Lando D, Voelker T A
Roussel Uclaf, 102 Route De Noisy, F 93230 Romainville, France.
Plant Physiol. 1991 Jun;96(2):473-8. doi: 10.1104/pp.96.2.473.
We have purified the protein for the enzyme sucrose phosphate synthase (SPS) from corn (Zea mays) leaves. Partially purified SPS protein was used to generate specific monoclonal antibodies. The following immunoaffinity chromatography allowed the isolation of pure SPS protein. The apparent molecular mass of the SPS polypeptide is 138 kilodaltons. By immunoblot, an SPS antigen was found to accumulate in mature leaves. SPS protein levels remain constant during the day/night cycle. The observed diurnal fluctuation of extractable enzyme activity, therefore, must be caused by modification of the specific activity of SPS in vivo.
我们已经从玉米(Zea mays)叶片中纯化出了蔗糖磷酸合酶(SPS)的蛋白质。部分纯化的SPS蛋白被用于制备特异性单克隆抗体。随后的免疫亲和层析实现了纯SPS蛋白的分离。SPS多肽的表观分子量为138千道尔顿。通过免疫印迹法发现,SPS抗原在成熟叶片中积累。SPS蛋白水平在昼夜循环中保持恒定。因此,观察到的可提取酶活性的昼夜波动必定是由体内SPS比活性的改变引起的。