Thermodynamic Criteria for the Removal of Certain Hepatic Insufficiency Markers from Protein-Containing Solutions

Николаев, В. Г.; Sarnatskaya, V. V.; Ivanyuk, Anton; Yushko, L. A.

doi:10.1007/978-3-642-77359-4_15

Cited by 7 publications

(5 citation statements)

References 2 publications

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“…The melting temperature of blood plasma proteins (BPP), serving as an integral criterion for degree of their ligand loading, has been previously reported [33]. In this study, the comparison of melting thermograms of BPP showed the differences in their shape and positions of peaks ( Figure 13).…”

Section: Resultssupporting

confidence: 50%

The effect of two formulations of carbon enterosorbents on oxidative stress indexes and molecular conformation of serum albumin in experimental animals exposed to CCl4

Sarnatskaya

Mikhailenko

Prokopenko

et al. 2020

Heliyon

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The liver failure means inability to perform its normal synthetic, biotransformation and excretory functions. The disturbance of metabolic processes leads to the development of "metabolic endogenous intoxication" resulting in oxidative stress. Oxidative stress initiates the processes of oxidation of amino acid residues of blood plasma proteins causing the changes in their structure and functions. The effect of administration of highly activated porous carbonic enterosorbents on oxidative stress manifestations and molecular conformation of serum albumin in blood of experimental animals with acute liver failure induced by carbon tetrachloride (CCl 4) needs to be investigated. Two forms of activated carbonic enterosorbents such as AC1 (primary beads with the range of diameters of 125-250 μm) and AC2 (secondary granules prepared from micronized AC1 having the mean particle size of~1 μm) derived from phenol-formaldehyde resin were used in rat model with CCl 4 intoxication. The total level of reactive oxygen species (ROS) in blood plasma, the activity of catalase (CAT) in blood hemolysates; the content of reduced glutathione (GSH) in liver homogenates, and the level of oxidative modification of proteins (OMP) such as aldehyde-dinitrophenylhydrazone (A-DNPH) and ketone-dinitrophenylhydrazone (K-DNPH) derivatives in blood plasma and liver homogenates were determined. In addition, the level of pro/antioxidant ratio in blood hemolysates and the content of lipid peroxidation product-malondialdehyde (MDA), in blood plasma and liver were determined. Melting thermograms of blood plasma proteins (BPP) and molecular conformation changes of serum albumin were analyzed by biophysical methods (differential scanning microcalorimetry and spectrofluorimetry). The extent of CCl 4-induced oxidative damage in blood and liver of experimental animals was shown to be less expressed for AC1 in comparison with AC2 enterosorbent. However, AC2 used in the form of secondary granules positively influenced some biophysical properties of albumin molecule (temperature of melting, shape of melting endotherm and intrinsic fluorescence) after rats exposure to CCl 4. In general, administration of both AC1 and AC2 led to the reduction of oxidative stress manifestations and partial restoration of native molecular conformation of serum albumin. These observations are promising in terms of achieving recovery of detoxification potential of organism after severe liver injury.

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Section: Resultssupporting

confidence: 50%

The effect of two formulations of carbon enterosorbents on oxidative stress indexes and molecular conformation of serum albumin in experimental animals exposed to CCl4

Sarnatskaya

Mikhailenko

Prokopenko

et al. 2020

Heliyon

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“…Initially we demonstrated that the human albumin isolated from the sera and plasma of one donor had the same thermodynamic and fluorescence characteristics (unpublished data). Melting thermograms of healthy do-nors and uremic HSA were recorded on a differential adiabatic scanning microcalorimeter (IIASM-4; Biopribor, Russia) by a procedure described earlier (17). The purity of the preparations measured electrophoretically with sodium dodecyl sulfate was more than 95%.…”

Section: Patients Materials and Methodsmentioning

confidence: 99%

“…Other reagents were analytically pure and used without additional purification. Melting thermograms of healthy do-nors and uremic HSA were recorded on a differential adiabatic scanning microcalorimeter (IIASM-4; Biopribor, Russia) by a procedure described earlier (17). Mathematical deconvolution of HSA endotherms was performed by Privalov and Potekhin (18) into two components which is more suitable according to the concept of mechanisms involved in the generation of bimodal HSA melting curves (19,20).…”

Section: Patients Materials and Methodsmentioning

confidence: 99%

Biophysical Studies on the Correction of Uremic Human Serum Albumin Binding Defects by In Vitro Charcoal Adsorption Treatment

Vg¹,

Sarnatskaya²,

Appen³

et al. 1996

Artificial Organs

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Spectrofluorimetry, flow microcalorimetry, and differential scanning microcalorimetry (DSMC) were used to study the conformation, binding function, and ligand loading of uremic albumin obtained from the blood plasma of 2 end-stage renal disease (ESRD) patients before and after charcoal plasma treatment at different pH values (3.0-9.0). The spectrofluorimetric patterns of conformational N-F transition at low pH (4.2-3.5) are practically identical for both samples of uremic human serum albumin (HSA) and control HSA from healthy donors. After the charcoal treatment at pH 3.0 and 4.0, the enthalpies of complexing on uremic HSA with bromsulfalein and sodium dodecylsulfate approach that of donor HSA. The binding affinity of uremic HSA for sodium octanoate, phenol red, and salicylic acid following low pH charcoal treatment even exceed those of donor HSA. At the same time the charcoal treatment of uremic plasma at neutral and alkaline pH does not notably improve the binding characteristics of isolated HSA. Adsorption at low pH values completely restores the tryptophan fluorescence spectrum position of uremic albumin and improves the thermodynamic characteristics of its melting process. Using DSMC data, it can nevertheless be concluded that some conformational changes or a certain amount of high-affinity bound endogenous ligands still remain after low pH uremic HSA purification. The latter conclusion requires additional improvements of adsorption treatment of uremic plasma.

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“…The range of scanning temperatures was 3O0-1O0"C, cell volume 0.5 ml, protein concentration 5 mg/ml on a serum albumin basis; a phosphate buffer (0.05 M , pH 7.1) was used as a medium; the heating rate was 1"Cimin. The shifts of HSA melting curves to the right along the temperature axis and pronounced bimodality were interpreted as a result of loading of this protein with tightly bound ligands (12,13). The thermal effect of protein complexing with sodium octanoate, phenol, sodium deoxycholate, and methyl red was recorded by a TAM-2277 flow microcalorimeter (LKB, Sweden).…”

Section: Methodsmentioning

confidence: 99%

Peritoneal Dialysis for the Removal of Protein‐Bound Markers of Hepatic Insufficiency

et al. 1993

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The addition of human serum albumin (HSA) to peritoneal dialysate increases the clearance of bilirubin in rats suffering from obstructive jaundice. The acceptor properties of the fluid can be enhanced by using HSA that does not contain standard stabilizing additives and has been purified by further adsorption on activated carbon. Bilirubin‐containing dialysate fluid, as well as the ascitic fluid of cirrhotic patients, can be regenerated by a combination of membrane ultrafiltration and carbon adsorption. These observations suggest a potentially useful scheme for continuous, regenerative peritoneal dialysis in the treatment of hepatic insufficiency.

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Thermodynamic Criteria for the Removal of Certain Hepatic Insufficiency Markers from Protein-Containing Solutions

Cited by 7 publications

References 2 publications

The effect of two formulations of carbon enterosorbents on oxidative stress indexes and molecular conformation of serum albumin in experimental animals exposed to CCl4

The effect of two formulations of carbon enterosorbents on oxidative stress indexes and molecular conformation of serum albumin in experimental animals exposed to CCl4

Biophysical Studies on the Correction of Uremic Human Serum Albumin Binding Defects by In Vitro Charcoal Adsorption Treatment

Peritoneal Dialysis for the Removal of Protein‐Bound Markers of Hepatic Insufficiency

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