Research Institute for Biochemical Regulation, School of Agriculture, Nagoya University, Chikusa, Nagoya 464, Japan.
Plant Physiol. 1978 Jul;62(1):97-100. doi: 10.1104/pp.62.1.97.
Spinach leaf (Spinacia oleracea L. var. Kyoho) protoplasts sustain protein-synthesizing activity as measured by the incorporation of [(14)C]-leucine into the protein fraction both in the light and in the dark. By the immunoprecipitation of ribulose-1,5-bisphosphate (RuP(2)) carboxylase with rabbit antibody raised against the purified spinach enzyme preparation, it was found that approximately 7% of the total radiocarbon incorporated into the protein fraction in the light was in the carboxylase molecules. However, there was no measurable net increase observed in the content of the enzyme protein in the experimental conditions employed. It was found that both chloramphenicol and cycloheximide inhibited the incorporation of [(14)C]leucine into RuP(2) carboxylase and its constituent subunits, as measured by the immunoprecipitation of the enzyme molecule and its subunits, A and B.
菠菜叶（Spinacia oleracea L. var. Kyoho）原生质体在光照和黑暗条件下均能维持蛋白质合成活性，这可通过将 [(14)C]-亮氨酸掺入蛋白质部分来衡量。通过用兔抗纯化的菠菜酶制剂制备的抗体对核酮糖-1,5-二磷酸 (RuP(2)) 羧化酶进行免疫沉淀，发现约 7%的总放射性碳掺入到光下的蛋白质部分中是在羧化酶分子中。然而，在所用的实验条件下，没有观察到酶蛋白含量的可测量净增加。发现氯霉素和环己酰亚胺均能抑制 [(14)C]亮氨酸掺入 RuP(2) 羧化酶及其组成亚基，这可通过酶分子及其亚基 A 和 B 的免疫沉淀来衡量。
