Araki K, Nakanishi H, Hirano H, Kato M, Sasaki T, Takai Y
Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita, Japan.
Biochem Biophys Res Commun. 1995 Jun 6;211(1):296-305. doi: 10.1006/bbrc.1995.1810.
A new Rab GDI was purified from the synaptic soluble fraction of rat brain by several column chromatographies as a protein that inhibited the dissociation of [3H]GDP from Rab3A but was not recognized by an anti-Rab GDI alpha antibody. The partial amino acid sequence analysis revealed that it was identical with rat Rab GDI beta. Purified Rab GDI beta showed the kinetic properties similar to those of Rab GDI alpha, including the inhibitory effect on the dissociation of GDP from Rab3A, the substrate specificity, the requirement of the post-translational lipid modifications of Rab3A, the stoichiometric interaction with the GDP-bound form of Rab3A, the inhibitory effect on the binding of Rab3A to erythrocyte ghosts, and the stimulatory effect on the dissociation of Rab3A from the membrane.
通过多种柱色谱法从大鼠脑突触可溶性组分中纯化出一种新的Rab GDI，它作为一种蛋白质可抑制[3H]GDP从Rab3A上解离，但不被抗Rab GDIα抗体识别。部分氨基酸序列分析表明它与大鼠Rab GDIβ相同。纯化的Rab GDIβ表现出与Rab GDIα相似的动力学特性，包括对GDP从Rab3A上解离的抑制作用、底物特异性、Rab3A翻译后脂质修饰的需求、与GDP结合形式的Rab3A的化学计量相互作用、对Rab3A与红细胞膜结合的抑制作用以及对Rab3A从膜上解离的刺激作用。
