. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. ADP-RIBOSYLATION OF G PROTEINS 351 36 Mr Ve Sc Ro Pat 43 29 Figure 5. Immunoblots of Sebastolobus alim' (Ve), 5. alascanus (Sc). Anlimnra rosirata (Ro). and Ratlus minis (Rat) brain membranes obtained using a peptide antiserum (MS/1) which recognizes the pi subunit (36 kDa) ofG proteins. proximately 39 kDa in rat brain membranes, but two im- munoreactive proteins were detected in all three marine fishes. In addition to a heavily stained band of approxi- mately 39 kDa. which likely represents G0ll, brain mem- branes from
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. ADP-RIBOSYLATION OF G PROTEINS 351 36 Mr Ve Sc Ro Pat 43 29 Figure 5. Immunoblots of Sebastolobus alim' (Ve), 5. alascanus (Sc). Anlimnra rosirata (Ro). and Ratlus minis (Rat) brain membranes obtained using a peptide antiserum (MS/1) which recognizes the pi subunit (36 kDa) ofG proteins. proximately 39 kDa in rat brain membranes, but two im- munoreactive proteins were detected in all three marine fishes. In addition to a heavily stained band of approxi- mately 39 kDa. which likely represents G0ll, brain mem- branes from the marine teleosts displayed immunoreactive proteins of apparent molecular masses of 41 to 42 kDa. There were no significant differences between the two Se- bastolobus species in the intensity of immunoreactive bands detected with the antiserum GC/2 (Table II). The antipeptide antiserum AS/7 was used to identify Gu,i and G,,,;. These a subunits in rat brain were readily resolved in the presence of 4 M urea in the running gel (Fig. 4). This doublet was not resolved as well in the three marine fishes, where the band tentatively identified as G,,,: migrated somewhat slower than the corresponding protein in rat brain membranes. There were no significant differ- ences in the levels of Gi(ll or G,l>2 between the Sebastolobus species (Table 11). Immunoblots of G protein /? subunits are depicted in Figure 5. The antiserum MS/1 was used to quantify the 36 kDa ft subunits. and the intensity of these bands did not differ significantly between the Sehastolohus species (Table 11). The substrate for the pertussis toxin-catalyzed ADP- ribosylation reaction is the heterotrimeric holoprotein (Neer et 1984; Van Dop el ai. 1984), and as a con- sequence, guanyl nucleotides are capable of modulating the sensitivity of G proteins to pertussis toxin (, Gier- schik. 1992). We therefore compared the guanyl nucleo- tide regulation of ADP-ribosylation in S. altivelis and S. alascanus. The a
Size: 1546px × 1615px
Photo credit: © Library Book Collection / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
