Transfer of egg white proteins with reference to lysozyme during the development ofMeleagris gallopavo(Galliformes: Phasianidae) embryos
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چکیده
منابع مشابه
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...
متن کاملPrecursor of Egg White Lysozyme
Lysozyme mRNA was translated in a reticulocyte lysate with mixtures of radioactive amino acids. The in vitro product isolated by immunoprecipitation was shown by gel electrophoresis, peptide mapping, and sequence analysis to be larger than lysozyme synthesized in uiuo. An NH,-terminal extension was completely sequenced by automated Edman degradation; the phenylthiohydantoins from each cycle wer...
متن کاملHen 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 ...
متن کاملThermal 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...
متن کاملCharacterization 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...
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ژورنال
عنوان ژورنال: Italian Journal of Zoology
سال: 2015
ISSN: 1125-0003,1748-5851
DOI: 10.1080/11250003.2015.1060268