Degradation Products Of Ccda And Ccda41 Ccda Upper Profile In Both

Degradation Products Of Ccda And Ccda41 Ccda Upper Profile In Both Fig. 5 degradation products of ccda and ccda41. ccda (upper profile in both panels) or ccda41 (lower profile in both panels) was incubated with lon; samples were quenched in guanidine hcl, and peptide products were separated by reverse phase chromatography. ccda was degraded in the presence of atp, and ccda41 was degraded in the presence of amppnp. 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.

Analysis Of Ccda And Ccda41 Degradation By Sds Page Ccda 5 G Or 5. degradation products of ccda and ccda41. ccda (upper profile in both panels) or ccda41 (lower profile in both panels) was incubated with lon; samples were quenched in guanidine hcl, and peptide products were separated by reverse phase chromatography. ccda was degraded in the presence of atp, and ccda41 was degraded in the presence of amppnp. Ondary structure of both proteins. fig. 4 shows the circular analysis of ccda and ccda41 degradation by sds page.ccda(5mg)orccda41(2mg)wasincubatedwithlon(2mg)and. Degradation products of ccda and ccda41. ccda (upper profile in both panels) or ccda41 (lower profile in both panels) was incubated with lon; samples were quenched in guanidine hcl, and peptide. 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.

Circular Dichroism Of Ccda And Ccda41 Spectra Of Protein Samples In 10 Degradation products of ccda and ccda41. ccda (upper profile in both panels) or ccda41 (lower profile in both panels) was incubated with lon; samples were quenched in guanidine hcl, and peptide. 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. Ccda, the antidote protein of the ccd post segregational killing system carried by the f plasmid, was degraded in vitro by purified lon protease from escherichia coli. ccda had a low affinity for lon (km≥200 µm), and the peptide bond turnover number was ∼10 min−1. ccda formed tight complexes with purified ccdb, the killer protein encoded in the ccd operon, and fluorescence and. Similarly, in the ccd system, we found that tldd and tlde are involved in ccda and ccda41 antidote degradation rather than being involved in the ccdb resistance mechanism. interestingly, sequence database comparisons revealed that these two proteins have homologues in eubacteria and archaebacteria, suggesting a broader physiological role.