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Title: Purification of GTPase-activating protein specific for the rho gene products. Author: Morii N, Kawano K, Sekine A, Yamada T, Narumiya S. Journal: J Biol Chem; 1991 Apr 25; 266(12):7646-50. PubMed ID: 1902224. Abstract: A GTPase-activating protein specific for the rho gene products (rho-GAP) was purified from the cytosol of bovine adrenal gland. Purification procedures consisted of ammonium sulfate fractionation, chromatographies on columns of phenyl-Sepharose and CM-Sepharose, gel filtration on a TSK-gel G3000SW, and Mono S fast protein liquid chromatography. By these procedures the activity was purified about 36,000-fold with a recovery of 0.6%. The final preparation showed a major protein band at Mr 28,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stimulated GTP hydrolysis by the purified rho A protein in a time- and dose-dependent manner. No stimulation was found for ras p21. The ADP-ribosylation on the rho protein by botulinum C3 exoenzyme did not affect its interaction with the purified rho-GAP.[Abstract] [Full Text] [Related] [New Search]