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This research aims to purify and characterize a protein that inhibits GDP dissociation from smg p25A, a GTP-binding protein.

Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein.

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Purification reveals a novel protein that inhibits GDP dissociation and GTP binding in smg p25A, suggesting new regulatory mechanisms.

This research aims to purify and characterize a protein that inhibits GDP dissociation from smg p25A, a GTP-binding protein.
Protein purified from bovine brain cytosol to near homogeneity.
Characterization through sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration.
Analysis of the effects on GDP and GTP binding.
smg p25A GDP dissociation inhibitor (GDI) inhibits GDP dissociation from smg p25A.
GDI inhibits binding of GTPgamma S to GDP-bound smg p25A (no effect on guanine nucleotide-free form).
GDI has a Mr of about 54,000 to 82,000 and an isoelectric point of about pH 5.6.

Sasaki et al. (1990) studied this question.

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