Western Blot Analysis Of Ccda41 And Ccda A Analysis Of Ccda41 And Fig. 3 analysis of ccda and ccda41 degradation by sds page. ccda (5 µg) or ccda41 (2 µg) was incubated with lon (2 µg) and the indicated nucleotide, with or without an atp regenerating system (rs) as described under “experimental procedures.” the reactions were stopped by boiling in sds. Download scientific diagram | analysis of ccda and ccda41 degradation by sds page. ccda (5 g) or ccda41 (2 g) was incubated with lon (2 g) and the indicated nucleotide, with or without an atp.
Analysis Of Ccda And Ccda41 Degradation By Sds Page Ccda 5 G Or Fig. 3. analysis of ccda and ccda41 degradation by sdspage. ccda (5 mg) or ccda41 (2 mg) was incubated with lon (2 mg) and the indicated nucleotide, with or without an atp regenerating system (rs) as described under “experimental procedures.” the reactions were stopped by boiling in sds. a, incubations of ccda; b, incubations of ccda41. Ccda41 eluted at 26.8 min and ccda eluted at 31.5 min. b, profile of cleavage products from ccda41 or ccda after degradation by lon. size by sds page analysis. identity of ccda was confirmed by. A, ccda or ccda41 without treatment. ccda41 eluted at 26.8 min and ccda eluted at 31.5 min. b, profile of cleavage products from ccda41 or ccda after degradation by lon. from publication: atp. Purified ccda and synthetic ccda41, consisting of the carboxyl terminal 41 amino acids of ccda, were degraded by lon protease as described by van melderen et al. (7). for quantitation of ccda and ccda41 degradation, the reactions were quenched with 4 m guanidine hcl and degradation products were analyzed by reverse phase chroma.
Sds Page Followed By In Situ Cmcase Activity Staining A And A, ccda or ccda41 without treatment. ccda41 eluted at 26.8 min and ccda eluted at 31.5 min. b, profile of cleavage products from ccda41 or ccda after degradation by lon. from publication: atp. Purified ccda and synthetic ccda41, consisting of the carboxyl terminal 41 amino acids of ccda, were degraded by lon protease as described by van melderen et al. (7). for quantitation of ccda and ccda41 degradation, the reactions were quenched with 4 m guanidine hcl and degradation products were analyzed by reverse phase chroma. Lon cleaved ccda primarily between aliphatic and hydrophilic residues, and ccda41 was cleaved at the same peptide bonds, indicating that atp hydrolysis does not affect cleavage specificity. ccda lost alpha helical structure at elevated temperatures (tm approximately 50 degrees c), and its degradation became independent of atp hydrolysis at this. Degradation of ccda (which requires unfolding) but not of ccda41 (which does not require unfolding) was inhibited, suggesting that pina inhibits the chaperone activity of lon. we propose that pina prevents the unfolding of protein substrates by interfering with atp hydrolysis and the conformational changes in lon that accompany atp hydrolysis.
Circular Dichroism Of Ccda And Ccda41 Spectra Of Protein Samples In 10 Lon cleaved ccda primarily between aliphatic and hydrophilic residues, and ccda41 was cleaved at the same peptide bonds, indicating that atp hydrolysis does not affect cleavage specificity. ccda lost alpha helical structure at elevated temperatures (tm approximately 50 degrees c), and its degradation became independent of atp hydrolysis at this. Degradation of ccda (which requires unfolding) but not of ccda41 (which does not require unfolding) was inhibited, suggesting that pina inhibits the chaperone activity of lon. we propose that pina prevents the unfolding of protein substrates by interfering with atp hydrolysis and the conformational changes in lon that accompany atp hydrolysis.
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