Purification and characterization of rab GDIβ from rat brain

Keishi Araki; Hiroyuki Nakanishi; Hisanobu Hirano; Masaki Kato; Takuya Sasaki; Yoshimi Takai

doi:10.1006/bbrc.1995.1810

Purification and characterization of rab GDIβ from rat brain

Keishi Araki, Hiroyuki Nakanishi, Hisanobu Hirano, Masaki Kato, Takuya Sasaki, Yoshimi Takai

Research output: Contribution to journal › Article › peer-review

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Abstract

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 GDIα antibody. The partial amino acid sequence analysis revealed that it was identical with rat Rab GDIβ. Purified Rab GDIβ showed the kinetic properties similar to those of Rab GDIα, 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.

Original language	English
Pages (from-to)	296-305
Number of pages	10
Journal	Biochemical and Biophysical Research Communications
Volume	211
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.1995.1810
Publication status	Published - Jun 6 1995
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.1995.1810

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abstract = "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 GDIα antibody. The partial amino acid sequence analysis revealed that it was identical with rat Rab GDIβ. Purified Rab GDIβ showed the kinetic properties similar to those of Rab GDIα, 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.",

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AU - Araki, Keishi

AU - Nakanishi, Hiroyuki

AU - Hirano, Hisanobu

AU - Kato, Masaki

AU - Sasaki, Takuya

AU - Takai, Yoshimi

PY - 1995/6/6

Y1 - 1995/6/6

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AB - 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 GDIα antibody. The partial amino acid sequence analysis revealed that it was identical with rat Rab GDIβ. Purified Rab GDIβ showed the kinetic properties similar to those of Rab GDIα, 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.

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Purification and characterization of rab GDIβ from rat brain

Abstract

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