Gn‐proteins are distinct from ras p21 and other known low molecular mass GTP‐binding proteins in the platelet

FEBS Letters

Haslam, Richard J.¹  Bhullar, Rajinder P.¹ 

[1] Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada

关键词: Gn-protein;    GTP-binding protein;    ras p21 protein;    Botulinum neurotoxin;    Platelet;    Gn-proteins;    23–27 kDa proteins detected by binding of [32P]GTP to nitrocellulose blots [1]. A pertussis toxin-sensitive neutrophil G-protein with an α-subunit of 40 kDa has also been designated Gn [2];    but is probably identical to Gi2 [3];   

DOI  :  10.1016/0014-5793(88)80194-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 27 kDa platelet membrane protein (G_n27) that binds [α-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 G_n27. A low molecular mass GTP-binding protein from bovine brain [(1987) Biochem. J. 246, 431–439] was also resolved from G_n27. At the levels normally present in cell membranes, only G_n-proteins bound significant amounts of [³²P]GTP after transfer of protein from SDS-polyacrylamide gels to nitrocellulose.

【 授权许可】

Unknown