Abstract
Two major G n-proteins, G n27 and G n26, were detected in the 100,000 × g av particulate fraction of rabbit and bovine brain. The G n26 protein was also present in significant amounts (∼50% of total) in the brain supernatant fraction. An antiserum raised against recombinant simian ralA recognized a 27-kDa brain protein with the same apparent molecular mass as the G n27 protein. In further analysis by two-dimensional polyacrylamide gel electrophoresis, the brain particulate G n-proteins were resolved into 6 major forms, four of 27 kDa (G n27 a–d) and two of 26 kDa (G n26 a and G n26 b). Minor GTP-binding components were also observed at 25 kDa and 24 kDa. The ratA antibody reacted strongly with the brain G n27 b form and weakly with the G n27 a and G n27 c but not with G n27 d or any of the other G n-proteins. In addition, comparison of human platelet and bovine brain particulate G n-proteins by two-dimensional polyacrylamide gel electrophoresis demonstrated a tissue/cell-type specific expression of the various forms of G n-proteins.
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