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G n ‐proteins are distinct from ras p21 and other known low molecular mass GTP‐binding proteins in the platelet
Author(s) -
Bhullar Rajinder P.,
Haslam Richard J.
Publication year - 1988
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(88)80194-7
Subject(s) - gtp' , molecular mass , g protein , platelet , polyacrylamide gel electrophoresis , blot , chemistry , nitrocellulose , biochemistry , gtp binding protein regulators , membrane , membrane protein , platelet lysate , microbiology and biotechnology , gel electrophoresis , binding protein , receptor , biology , in vitro , enzyme , gene , immunology
The 27 kDa platelet membrane protein (G n 27) that binds [α‐ 32 P]GTP on nitrocellulose blots of SDS‐polyacrylamide gels [(1987) Biochem. J. 245, 617–620] was compared with other low molecular mass GTP‐binding proteins. Platelet membranes also contained 21 kDa proteins that bound anti‐ ras p21 antibody and 22–23 kDa proteins that could be ADP‐ribosylated by botulinum neurotoxin type D. These groups of proteins were resolved electrophoretically from each other and from G n 27. A low molecular mass GTP‐binding protein from bovine brain [(1987) Biochem. J. 246, 431–439] was also resolved from G n 27. At the levels normally present in cell membranes, only G n ‐proteins bound significant amounts of [ 32 P]GTP after transfer of protein from SDS‐polyacrylamide gels to nitrocellulose.