Gn-proteins are distinct from ras p21 and other known low molecular mass GTP-binding proteins in the platelet.
The 27 kDa platelet membrane protein (Gn27) that binds [alpha-32P]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 Gn27. A low molecular mass GTP-binding protein from bovine brain [(1987) Biochem. J. 246, 431-439] was also resolved from Gn27. At the levels normally present in cell membranes, only Gn-proteins bound significant amounts of [32P]GTP after transfer of protein from SDS-polyacrylamide gels to nitrocellulose.
D001792:Blood Platelets / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000097:blood* / Q000302:isolation & purification; D006160:Guanosine Triphosphate / Q000097:blood*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood* / Q000302:isolation & purification; D008970:Molecular Weight; D011518:Proto-Oncogene Proteins / Q000097:blood* / Q000302:isolation & purification; D016283:Proto-Oncogene Proteins p21(ras)
D008565:Membrane Proteins; D011518:Proto-Oncogene Proteins; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)