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Identification of some of the brain G n 27 as the ral gene product Comparison between the brain and platelet G n ‐proteins
Author(s) -
Bhullar Rajinder P.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80022-9
Subject(s) - g protein , gel electrophoresis , polyacrylamide gel electrophoresis , microbiology and biotechnology , recombinant dna , molecular mass , antiserum , platelet , gtp' , biology , chemistry , biochemistry , two dimensional gel electrophoresis , gene , antibody , proteomics , enzyme , receptor , immunology
Two major G n ‐proteins, G n 27 and G n 26, were detected in the 100,000 × g av particulate fraction of rabbit and bovine brain. The G n 26 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 n 27 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 n 27 a–d ) and two of 26 kDa (G n 26 a and G n 26 b ). Minor GTP‐binding components were also observed at 25 kDa and 24 kDa. The ratA antibody reacted strongly with the brain G n 27 b form and weakly with the G n 27 a and G n 27 c but not with G n 27 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.