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To investigate the change of the down-stream apoptostic protein after expressions of PrP mutants, the cellular level of pro-caspase-3 protein in each preparation was detected by Western blot.
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Antibodies against TG antigen preparation were detected in 52 (14.5%, 95%CI11.0%0%–18.6%) of 357 specimens tested; 47 (90.4%) of these specimens that reacted to TG antigens were also positive for SFG antigens, and 5 (1.4%) of the 357 specimens were positive for TG antigens alone.
In 32 sera (88.9%), antibodies reactive with both preparations were detected.
No improvement in the enzymatic preparation activity was detected upon addition of CBM-SUMO when the soluble carboxymethyl cellulose was used as substrate.
On a parallel Western blot loaded with VLPs from the same sample preparation, p24 was detected using pooled plasma of HIV-1+ individuals, confirming the presence of p24 in all samples.
Mild proteolysis process followed by PNGase F digestion showed that in addition to the 25 kDa band that presented in all preparation, an 18 kDa PrP-specific band was detected in the preparations of PrP-A117V and PrP-G114V (Fig. 7A), which occupied about 34% and 37% of total PrPs after digitalizing the signal intensities, respectively (Fig. 7B).
Similar IgE-binding was observed for all egg white preparations, while an elevated allergenicity was detected in egg yolk from Araucana chicken.
In addition, SR-BI was detected in preparations of rat liver canalicular membranes.
A decrease in the voltammetric charge was detected as the preparation temperature increased, which could be related to the crystallization process and reduction of the surface area of the layer.
Also in the RW10S2 tailocin preparation, the com-linked cargo protein was detected (fig. 2).
No endotoxin was detected in protein preparations, as determined by the Limulus Amebocyte Lysate test from Sigma.
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