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Updated: Aug 9, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
Pertussis toxin-sensitive GTP-binding proteins characterized in synaptosomal fractions of embryonic avian cerebral
1Diabetes Unit, Massachusetts General Hospital, Harvard Medical School, Boston 02114, USA. holz@helix.mgh.harvard.edu
Abstract:
Pertussis toxin (PTX)-sensitive GTP-binding proteins (G proteins) are essential intermediaries subserving neuronal signal transduction pathways that regulate excitation-secretion coupling. Despite this established role, relatively little is known regarding the identity, subcellular distribution, and relative abundance of this class of G proteins in synaptic nerve endings. Here, sucrose density gradient centrifugation was combined with 1- and 2-dimensional gel electrophoresis to characterize PTX-sensitive G protein alpha subunits in synaptosomal fractions of embryonic (day 12) chick cerebral cortical homogenates. These findings demonstrate multiple isoforms of M(r) 40-41 kDa Gi alpha and G(o) alpha subunits that can be identified on the basis of PTX-catalyzed ADP-ribosylation and immunoblot analysis.
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