[38] Characterization of antibodies for various G-protein β and γ subunits
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A G protein γ subunit peptide stabilizes a novel muscarinic receptor state
2006, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The membranes were then washed twice with buffer A by centrifugation at 100,000g and were frozen at −85 °C until required. Immunoblot analysis with antibodies specific to the β1 subunit type [19], showed a significant decrease in that subunit after this treatment (data not shown). The amount of M2 receptor in our membrane stocks was determined by mixing serially diluted membrane stocks in buffer A with a saturating concentration of [3H]NMS (10 nM, final).
Regulation of angiotensin II-induced G protein signaling by phosducin-like protein
2002, Journal of Biological ChemistryCitation Excerpt :A cDNA construct encoding PhLP with a C-terminal c-Myc epitope tag was prepared and transiently expressed in CHO/AT1R cells. The fusion protein was immunoprecipitated with an anti-c-Myc antibody, and the precipitates were immunoblotted using antibodies specific to PhLP (29), Gβ1 (55), or Gqα family members (56). Fig.7 shows that Gβγ co-immunoprecipitated with PhLP whereas Gqα did not, suggesting a lack of high affinity interactions between PhLP and Gqα in these cells.
Role of the G protein γ subunit in βγ complex modulation of phospholipase Cβ function
2002, Journal of Biological ChemistryCitation Excerpt :First, we examined these βγ complexes using an assay that can detect gross changes in the conformation of the β subunit. The wild type βγ complex, when digested with trypsin, yields two fragments of ∼24 and 13 kDa as demonstrated before (31). Significant changes in the three-dimensional structure of the β subunit would be expected to generate other fragments on trypsin digestion due to the exposure of masked Lys and Arg residues.
Role of G protein βγ complex in receptor-G protein interaction
2002, Methods in EnzymologyG Protein β Subunit Types Differentially Interact with a Muscarinic Receptor but Not Adenylyl Cyclase Type II or Phospholipase C-β2/3
2001, Journal of Biological ChemistryCitation Excerpt :For initial expression studies, Sf9 cells were infected with the β4 virus for varying lengths of times. Cell lysates were examined by immunoblotting with B4-specific B4-2 antibody (27) used at 1:600 dilution. The purification of βγ subunits was performed essentially as described before (26).
Limited proteolytic digestion studies of G protein-receptor interactions
2000, Methods in Enzymology