Article
Guanine nucleotide binding properties of the mammalian RalA protein produced in Escherichia coli.
The Journal of biological chemistry - 15 Apr 1990
Frech M, Schlichting I, Wittinghofer A, Chardin P
Abstract excerpt
The simian ralA cDNA was inserted in a ptac expression vector, and high amounts of soluble ral protein were expressed in Escherichia coli. The purified p24ral contains 1 mol of bound nucleotide/mol of protein that can be exchanged against external nucleotide. The ral protein exchanges GDP with a t 1/2 of 90 min at 37 degrees C in the presence of Mg2+, and has a low GTPase activity (0.07 min-1 at 37 degrees C). We...
Topics
- Animals
- Base Sequence
- Binding Sites
- Escherichia coli
- GTP Phosphohydrolases
- GTP-Binding Proteins
- Genetic Vectors
- Guanine Nucleotides
- Guanosine Diphosphate
- Kinetics
- Magnesium Chloride