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Surg. 2015; 7: 370–377. 2 Schmid M, Schindler R, Weigand K, et al. Is albumin synthesis regulated by the colloid osmotic pressure? Effect of albumin and dextran on albumin and

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, inflammation causes hypoalbuminemia due to reduced synthesis and increased albumin catabolism. Serum albumin is the most important serum protein of human body. Serum albumin has not only vital functions but also has anti-atherogenic properties, including

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33 998 1012 Roche, M., Rondeau, P., Singh, N. R., Tarnus, E. and Bourdon, E. (2008): The antioxidant properties of serum albumin. FEBS Lett. 582

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Abstract  

Interaction of albumin with no-carrier-added metal radionuclides was studied in multielemental environment using dialysis technique. No-carrier-added 197mHg, 199–201Tl, 199–200Pb, 204Bi and 204,205Po were produced by irradiating Au target consecutively with 7Li and 12C beams. Similarly, 61Cu, 66–68Ga, 62,63Zn, 66,67,69Ge, 71,72As and 73Se were produced by irradiating cobalt target consecutively with 16O, 7Li and 12C projectiles. These no-carrier-added radionuclides were chemically separated from the bulk target before studying their interaction with albumin. It was found that Hg and Ga strongly bind with albumin, whereas Bi, Po, As, and Se do not bind at all with albumin. The binding affinities of Pb, Tl, Cu and Zn radionuclides towards albumin are moderate.

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2002 Beyond expansion: structural studies on the transport roles of human serum albumin DV Devine F Décary S

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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.

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Abstract  

Human serum albumin microspheres were labelled with99mTc as a single step kit with radiochemical yields higher than 95%. With respect to the organ distribution in mice, the per cent of injected dose in liver was 78%.

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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.

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–229. Klára, T., Csönge, L., Janositz, G., et al.: Albumin-coated structural lyophilized bone allografts: a clinikal report of 10 cases. Cell Tiss. Bank., 2014, 15 (1), 89–97. Ryser, M. F., Thieme, S., Bornhäuser, M., et

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Abstract  

Differential scanning calorimetry (DSC) has been employed to study the thermal denaturation processes of the main protein fractions of blood serum. These processes have been compared for albumins (nondefatted (HSA) and fatty acid free (HSAf)), α,β-globulins, γ-globulins, and their mixtures in aqueous (pH 6.5) and buffer (pH 7.2) solutions. The results have indicated that α,β-globulins inhibit γ-globulins’ aggregation in buffer solutions. The decrease of stability of HSA and HSAf aqueous solutions has been observed in the presence of γ-globulins. The mixtures of albumins and γ-globulins have revealed the tendency to ready aggregation in water. Moreover, the results have suggested that neither γ-globulins nor albumins severely change the stability of α,β-globulins.

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