Enzymatic Properties of Phosphoenolpyruvate Carboxylase of Purified Chloroplasts from CAM-Performing Kalanchoe blossfeldiana Poelln. Plants

スポンサーリンク

概要

• 論文の詳細を見る

• A phosphoenolpyruvate carboxylase (PEPC) (EC 4.1.1.3) activity was associated with, the Percoll purified chloroplasts from Kalanchoe blossfeldiana leaves performing crassulacean acid metabolism (CAM) (plants grown under short-day conditions). Very little PEPC activity was detected in the chloroplasts when the plants were grown under long days, performing a C_3-type photosynthetic metabolism. The PEPC activity measured in the chloroplasts from CAM-plants was very sensitive to such effectors as glucose-6-phosphate (G-6-P) and malate: the initial activity of PEPC in the presence of 1.2 mM PEP was 400% activated by 10 mM G-6-P and was 25% inhibited by 1 mM malate. These results show that the PEPC in the chloroplasts has the enzymatic characteristics described by Brulfert and Queiroz [(1982) Planta 154: 3391 for PEPC extracted from CAM-performing K. blossfeldiana leaves.

• 日本植物生理学会の論文

著者

• Rustin P

  Univ. Pierre Et Marie Curie Paris Fra

• Adam Veronique

  Universitd Pierre et Marie Curie, Laboratoire de Biologie Vegetale IV

• Rustin Pierre

  Universitd Pierre et Marie Curie, Laboratoire de Biologie Vegetale IV

• Adam Veronique

  Universitd Pierre Et Marie Curie Laboratoire De Biologie Vegetale Iv

関連論文

• Enzymatic Properties of Phosphoenolpyruvate Carboxylase of Purified Chloroplasts from CAM-Performing Kalanchoe blossfeldiana Poelln. Plants

スポンサーリンク