Maréchal E, Block M A, Joyard J, Douce R
Laboratoire de Physiologie Cellulaire Végétale, URA CNRS 576, Département de Biologie Moleculaire et Structurale, CEA-Centre d'Etudes Nucléaires de Grenoble, France.
FEBS Lett. 1994 Oct 3;352(3):307-10. doi: 10.1016/0014-5793(94)00978-3.
We have applied the 'membrane partition' kinetic modelling approach proposed by Heirwegh et al. [(1988) Biochem. J. 254, 101-108] to MGDG synthase in isolated envelope vesicles. Comparison of the kinetic parameters obtained for MGDG synthase assayed in purified envelope membranes and in mixed-micelles demonstrates that the latter are relevant to the situation in envelope membranes and that MGDG synthase has a very high affinity for dilinoleoylglycerol. Our results provide additional evidence for the hypothesis that the high affinity of the envelope MGDG synthase for dilinoleoylglycerol could be responsible for the presence of C18 fatty acids at both the sn-1 and sn-2 position of the glycerol backbone in MGDG.
我们已将Heirwegh等人提出的“膜分配”动力学建模方法（[(1988) Biochem. J. 254, 101 - 108]）应用于分离的包膜囊泡中的MGDG合酶。对在纯化的包膜膜和混合胶束中测定的MGDG合酶获得的动力学参数进行比较表明，后者与包膜膜中的情况相关，并且MGDG合酶对二亚油酰甘油具有非常高的亲和力。我们的结果为以下假设提供了额外的证据：包膜MGDG合酶对二亚油酰甘油的高亲和力可能是MGDG甘油主链的sn - 1和sn - 2位置都存在C18脂肪酸的原因。
