thermal aggregation of hen egg white lysozyme: effect of polyamines

Authors

bi bi fatemeh nobakht motlagh ghochani proteomics research center, faculty of paramedical sciences, shahid beheshti university of medical sciences, tehran

seyedeh zahra moosavi-nejad department of biology, faculty of basic sciences, alzahra university, tehran

abstract

protein aggregation is a serious problem for both biotechnology and cell biology. diseases such as prion misfolding, alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutations in the lysozyme gene. in this study, we investigated effect of small additives on the thermal aggregation of lysozyme. the main finding of this work is that multiple amine groups, spermine and spermidine, play pivotal roles in preventing the thermal aggregation of lysozyme. our results showed that effect of spermine is more than spermidine.

Upgrade to premium to download articles

Sign up to access the full text

Already have an account?login

similar resources

effect of polyamines on thermal inactivation of hen egg white lysozyme

lysozyme is considered as part of the innate immune system. it has stimulated considerable interest as a natural food preservative. lysozyme has been shown to be effective in preserving a variety of foods such as fresh fruits and vegetables, meats, seafood and wine, for which many japanese patents have been granted. the relatively high thermal stability of lysozyme also makes it attractive for ...

full text

Hen Egg - white Lysozyme Crystals

Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...

full text

Thermal aggregation of egg white proteins as affected by saccharides

Thermal characteristics of egg white proteins (EWP) may differ in the presence of saccharides. Therefore, the influence of saccharides including carboxymethyl cellulose (CMC), pectin, sucrose and maltodextrin and heating time on physicochemical characteristics of EWP as a whole were studied. Investigation of Heat Coagulation Time (HCT), solubility, turbidity and protein secondary structure of h...

full text

Study the Interaction of Ni Complex of Tetradentate Schiff Base Ligand with HEN Egg White Lysozyme

AbstractInteraction of Ni complex(Salen= N, N´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (HEWL) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. The protein binding affinity of Ni complex was found to be (3.0×103M−1). The binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 M...

full text

Characterization of the unfolding pathway of hen egg white lysozyme.

After the recent discovery of a ribonuclease A unfolding intermediate [Kiefhaber, T., et al. (1995) Nature 375, 513-515], we investigated the unfolding pathway of hen egg white lysozyme. At pH* 4.00 with D2O at 10 degrees C and 6 M guanidinium chloride, unfolding shows a single, slow kinetic phase, with a relaxation time of 3300 s when monitored by circular dichroism (CD). Exchange of the trypt...

full text

Refinement of triclinic hen egg-white lysozyme at atomic resolution.

X-ray diffraction data have been collected at both low (120 K) and room temperature from triclinic crystals of hen egg-white lysozyme to 0.925 and 0.950 A resolution, respectively, using synchrotron radiation. Data from one crystal were sufficient for the low-temperature study, whereas three crystals were required at room temperature. Refinement was carried out using the programs PROLSQ, ARP an...

full text

My Resources

Save resource for easier access later


Journal title:
journal of paramedical sciences

جلد ۴، شماره ۲، صفحات ۰-۰

Hosted on Doprax cloud platform doprax.com

copyright © 2015-2023