Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bhullar RP,Haslam RJdoi
10.1016/0014-5793(88)80194-7subject
Has Abstractpub_date
1988-09-12 00:00:00pages
168-72issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(88)80194-7journal_volume
237pub_type
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