Search Results

You are looking at 1 - 10 of 87 items for :

  • "bovine serum albumin" x
  • Refine by Access: All Content x
Clear All

Abstract  

A calorimetric study of thermal denaturation of bovine serum albumin in aqueous solutions has shown essential differences in stability of fatty acid containing and defatted albumin. The first one shows a single endotherm peak in DSC curve near 69°C with enthalpy change about 1000 kJ mol-1. Defated albumin melts in two different temperature ranges: near 56 and 69°C with enthalpy changes about 300 and 200 kJ mol-1 respectively. Deconvolution analysis shows that the single endotherm is well approximated as the sum of three independent two-state transitions. Two transitions of bimodal DSC curve for defatted albumin are not of a two-state type. This molecule melts probably as two structurally independent parts.

Restricted access

Abstract  

Protein unfolding events were studied by differential scanning calorimetry (DSC) for bovine serum albumin (BSA) aqueous solutions exposed to radio-frequency radiation. No immediate effect of this radiation on thermal unfolding of BSA was observed. The differences between irradiated and control samples have appeared during the storage of BSA solution. The irradiated samples changed faster than non-irradiated. Our results indicated that the age-related changes were stronger for 3.5 and 5 MHz than for 247 MHz frequency and dependent on energy power of radiation. Deconvolution of DSC traces allowed to study the effect of radio-frequency radiation on each component transition.

Restricted access

Summary The effect of pH on the thermal denaturation of BSA containing fatty acids was studied by use of differential scanning calorimetry (DSC). Thermal scanning of BSA aqueous solutions gave various types of DSC curves depending on the protein concentration and on the pH. The broad bimodal endothermic transition was suggested to be connected with loose protein structure in contradistinction to single peak for compact molecule structure. The propensity toward precipitation at pH conditions ranging from 3.8 to 5 was observed. A scan-rate independent and partly reversible behavior of the thermal heating of BSA was found. Deconvolution of DSC traces in non-two-state model with assumption of two- or three-component transition allowed to study the effect of pH on different parts of BSA molecule.

Restricted access

Abstract  

The thermal denaturation process of bovine and human both fatty acid containing and fatty acid free albumins in aqueous solution was studied by use of differential scanning calorimetry. Human serum albumins were found to be more stable than their bovine counterparts. Fatty acid free albumins were characterized as generally less stable, more susceptible to aggregation, their unfolding endothermic transition was less cooperative and with the smaller degree of reversibility. Deconvolution analysis with using a non-two-state model with two component transitions showed essential differences in the thermodynamic parameters between all studied albumins, particularly regarding the high-temperature component transition.

Restricted access

available since several companies have produced their own instruments. Herein, we summarized our own efforts on purification of six natural quinolone alkaloids from T. ruticarpum ( Figure 1 ) and evaluated their binding affinity for bovine serum albumin

Open access

Abstract  

The iodination and separation of various diagnostically and/or experimentally important peptides including (Tyr1)-somatostatin-14, rat Tyr-a-calcitonin gene-related peptide (23-37), motilin and vasoactive intestinal peptide, furthermore bovine serum albumin are described. All species were iodinated by the iodogen method. The 125I-labeled peptide products were separated by reversed-phase HPLC, the specific activities of mono-iodinated forms are near identical with the theoretical value. The labeled bovine serum albumin was separated by Sephadex G-100 gel filtration.

Restricted access
Journal of Thermal Analysis and Calorimetry
Authors: G. Barone, S. Capasso, P. Del Vecchio, C. De Sena, D. Fessas, C. Giancola, G. Graziano, and P. Tramonti

Abstract  

In a previous paper, we report a preliminary DSC study on bovine (BSA) and human (HSA) serum albumins. However, at accurate HPLC analysis the commercial proteins show three peaks: Fraction V-I, probably globulins (as declared by the producers), Fraction V-II (about 15–18% of the product) and Fraction V-III that represents pure BSA or HSA. A hypothesis is that the Fraction II is a covalent dimer, or trimer or a mixture of both, generated during the scalf-life of the commercial product. Denaturation enthalpies of the purified Fraction V-III and Fraction V-II of BSA, have been determined calorimetrically, at changing thepH, and the results of both compared with those obtained on the untreated protein. Few calorimetric experiments have been also carried on a BSA monomer derivative with sulphidril group protected. Computer program have been developed for the deconvolution of exo- and endothermic effects and for the analysis of thermal denaturation profiles.

Restricted access

Abstract  

The interactions of lanthanide ions (Ln3+) with bovine serum albumin (BSA) under mimetic physiological conditions (310.15 K, pH 6.7, 0.1MNaCl) were studied by microcalorimetry. For the first time, based on Two Sets of Independent Sites Model, molar enthalpies (Δr H m1, Δr H m2) and coordination number (n 1, n 2) of the two sets of binding sites with different affinity were obtained directly from the microcalorimetric results. It was shown that the interactions are endothermic and entropy-driving processes. By combining with fluorescence spectroscopy, other thermodynamic parameters (Δr G m1, Δr S m1) were determined for high-affinity specific sites.

Restricted access

Abstract  

Using the pulse radiolysis technique, the oxidation of the biological protein bovine serum albumin (BSA) by the species N 3 . , CCl3O 2 . , OH and Br 2 .– has been studied in aqueous solution. The repair of the N 3 . oxidation by ascorbic acid and the effect of denaturing the protein on this repair has also been studied. The oxidation of Br 2 .– seems to follow a different course from that of the other oxidizing agents suggesting the possibility of positive hole mobility in this protein. The repair by ascorbic acid is found more effective in the case of denatured protein. The rate constants for the reaction of Br 2 and N 3 . are lower, in general, in the case of the denatured protein as compared with the undenatured BSA both at pH 6.9 and pH 10.7, suggesting that the convoluted structure of the protein plays a part in the process.

Restricted access

Abstract  

The effect of glucose (0–15 mass%) on the kinetics of bovine serum albumin (BSA) denatured aggregation at high concentration in aqueous solution has been studied by differential scanning calorimetry. The observed denatured aggregation process was irreversible and could be characterized by a denaturation temperature (T m), apparent activation energy (E a), the approximate order of reaction, and pre-exponential factor (A). As the glucose concentration increased from 0 to 15 mass%, T m increased, E a also increased from 514.59409±6.61489 to 548.48611±7.81302 kJ mol−1, and A/s−1 increased from 1.24239E79 to 5.59975E83. The stabilization increased with an increasing concentration of glucose, which was attributed to its ability to alter protein denatured aggregation kinetics. The kinetic analysis was carried out using a composite procedure involving the iso-conversional method and the master plots method. The iso-conversional method indicated that denatured aggregation of BSA in the presence and absence of glucose should conform to single reaction model. The master plots method suggested that the simple order reaction model best describe the process. This study shows the combination of iso-conversional method and the master plots method can be used to quantitatively model the denatured aggregation mechanism of the BSA in the presence and absence of glucose.

Restricted access