Folding studies on muscle type of creatine kinase from Pelodiscus sinensis

Comparative studies of the expression of creatine kinase isoforms under immune stress in Pelodiscus sinensis

“…Previous reports have discussed the biochemical characteristics of PSCK in P. sinensis, mainly focusing on the muscle (PSCK-M) and brain (PSCK-B) types in vitro folding studies [15,16,20,21,29,30]. In this study, we have focused on the mitochondrial type such as PSCK-S and made a comparison between three types of PSCK isozymes.…”

“…The supernatant was obtained by freezing centrifugation at 5000 rpm for 15 min for biochemical parameters' assay. The total activity of PSCK from the tissues was measured following proton generation during the reaction of ATP and creatine with thymol blue at 597 nm and 25°C, as previously described [15,16,29,30]. The activities of total superoxide dismutase (T-SOD), lactate dehydrogenase assay (LDH), malondialdehyde (MDA), catalase (CAT), and the content of ATP were measured according to the kit manuals (A020-2 for LDH, A001-1 for T-SOD, A007-1 for CAT, A003-2 for MDA, and A095 for ATP) provided by Nanjing Jiancheng Biochemical Reagent Co. Ltd. (Nanjing, China) using the clinical biochemical indicator autoanalyzer: Infinite M200Pro spectrometer (Tecan, Switzerland), according to the manufacturer's instructions.…”

Hemoglobins Likely Function as Peroxidase in Blood ClamTegillarca granosaHemocytes

“…Differences in sensitivity and response pattern to Cu 2+ were observed between Tg-HbI and Tg-HbII which suggested that a more complex mechanism was likely involved in the response of Tg-Hbs to the metal ion. For the protein denaturants, SDS disrupts hydrophobic interactions in protein molecules, while urea interacts with amide groups and peptides to destabilize protein structures [ 20 ]. These interactions can change the conformations of Tg-Hbs, in particular the active center (i.e., the heme pocket), resulting in the loss of peroxidase activity.…”

“…These interactions can change the conformations of Tg-Hbs, in particular the active center (i.e., the heme pocket), resulting in the loss of peroxidase activity. It has been reported that sodium azide is a proven inhibitor of peroxidases including MPO and HRP, and the inactivation involves the binding of sodium azide to the heme, thus preventing substrates from oxidization [ 20 , 21 ].…”