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Identification of multiple ral gene products in human platelets that account for some but not all of the platelet G n ‐proteins
Author(s) -
Bhullar Rajinder P.,
Chardin Pierre,
Haslam Richard J.
Publication year - 1990
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(90)80063-o
Subject(s) - molecular mass , polyclonal antibodies , platelet , microbiology and biotechnology , polyacrylamide gel electrophoresis , isoelectric focusing , blot , antiserum , recombinant dna , membrane protein , gel electrophoresis , biochemistry , g protein , biology , gtp' , western blot , gtp binding protein regulators , chemistry , gene , antibody , receptor , membrane , genetics , immunology , enzyme
Polyclonal antibodies raised against specific recombinant low molecular mass GTP‐binding proteins were tested for their ability to recognize partially purified human platelet membrane G n ‐proteins (i.e. proteins that bind [α‐ 32 PlGTP on nitrocellulose blots of SDS/polyacrylamide gels). An antiserum against simian ral A protein recognized a 27 kDa human platelet protein with the same apparent molecular mass as the major platelet G n ‐protein (G n 27). In further analysis by two‐dimensional polyacrylamide gel electrophoresis, the isoelectric focusing step permitted resolution of 12 major G n ‐protein forms, seven of 27 kDa (G n 27a‐g), one of 26 kDa (G n 26) and four of 24 kDa (G n 24a‐d). The ral A antibody reacted strongly with the five most basic G n 27 species (a‐e), weakly with G n 26 and not at all with G n 27f, G n 27g or G n 24a‐d. We conclude that ral gene products account for some but probably not for all of the platelet G n ‐proteins.