Blood Serum Components Research Articles

Effects of Modified Detonation Nanodiamonds on the Biochemical Composition of Human Blood

In vitro experiments showed that protein and non-protein components of human blood serum could be absorbed on the surface of modified nanodiamonds obtained by detonation synthesis. The prospects of using nanodiamond as a new absorbent for hemodialysis, plasmapheresis, and laboratory diagnostics are discussed.

Transport of the anti-diabetic VO2 + complexes formed by pyrone derivatives in the blood serum

The biotransformation in the blood serum of the two anti-diabetic agents [VO(ema)2] – or BEOV – and [VO(koj)2] formed by ethylmaltol (Hema) and kojic acid (Hkoj) was studied with EPR spectroscopy, pH-potentiometry and DFT calculations. For comparison, the behavior of the systems with tropolone (Htrop) was also analyzed. The interaction of [VO(ema)2] and [VO(koj)2] with the most important bioligands of the serum, lactic (Hlact) and citric acid (H3citr), human serum transferrin (hTf), human serum albumin (HSA) and immunoglobulin G (IgG) was examined and discussed. Among the several mixed species observed, cis-VO(carrier)2(hTf), cis-VO(carrier)2(HSA) and cis-VO(carrier)2(IgG), where carrier is ethylmaltolate or kojate, with a His-N of the protein coordinated in the equatorial position, are plausible candidates for the transport processes of the drug toward the target organs. The values of the logβ are in the range 19.6–19.8 for the species formed by ethylmaltol and 17.4–17.6 for those formed by kojic acid. The formation of such species was confirmed through pH-titrations of the model systems VO2+/carrier/1-MeIm and VO2+/carrier/Ac-his, where 1-MeIm and Ac-his are 1-methylimidazole and N-acetylhistamine, and DFT calculations of 51V Az of the model species cis-[VO(carrier)2(1-MeIm)] and cis-[VO(carrier)2(Ac-his)]. The values of the stability constants for the mixed species observed were used to predict the biodistribution of VO2+ ion between the blood serum components for concentrations of 1, 10 and 50μM.

Abstracts of the 17th International Symposium on Bioluminescence and Chemiluminescence ‐ (ISBC 2012)

WARNING : The light-emitting molecular structures responsible for the chemiluminescence and fluorescence phenomena are not necessarily the same!

Study of the Ternary Complex Formation Between Vanadium(III), Dipicolinic Acid and Small Blood Serum Bioligands

Ternary complex formation reactions were studied between vanadium(III), dipicolinic acid and small molecular weight blood serum components: lactic, oxalic, citric and ortophosphoric acids. The electromotive force measurement permitted us to determine the chemical speciation of the complexes formed. In the vanadium(III)–dipicolinic acid–lactic acid system the complexes detected were: V(dipic)(lac), V(dipic)(lac)(OH)− and V(dipic)(lac)\((\mathrm{OH})_{2}^{2-}\). In the vanadium(III)–dipicolinic acid–oxalic acid system the observed complexes were: V(dipic)(ox)−, V(dipic)(ox)(Hox)2− and V(dipic)\((\mathrm{ox})_{2}^{3-}\). In the vanadium(III)–dipicolinic acid–citric acid system the complexes V(dipic)(Hcit)−, V(dipic)(cit)2−, V(dipic)(cit)(OH)3−, V(dipic)(cit)\((\mathrm{OH})_{2}^{4-}\) and V(dipic)(cit)\((\mathrm{OH})_{3}^{5-}\) were detected. Finally in the vanadium(III)–dipicolinic acid–phosphoric acid system the complexes V(dipic)(H2PO4) and V(dipic)(HPO4)− were observed. The UV-vis spectra allowed us to perform a qualitative characterization of the complexes formed in aqueous solution.

Study of some hematological and biochemical parameters of Rainbow trout (Oncorhynchus mykiss ) fry in western part of Mazandaran province, Iran

This study was done to investigate of some hematological and biochemical factors of rainbow trout (Oncorhynchus mykiss ) fry in west of Mazandaran in Iran. About 50 pools of blood samples from diseased fry were collected within 30 months from November 2002 till March 2005 from three hatchery farms in western part of Mazanderan province. In addition 30 pools of blood samples as control group were collected randomly from mentioned farms. Each blood samples were examined for whole blood examination and blood enzymes measurement. It consist of total leukocytes (WBC) and erythrocytes counts (RBC), hemoglobin (Hb) content, hematocrits (PCV), leukocytes differential count and blood indices such as MCV, MCH and MCHC. Also blood serums were analysed for total protein (TP) and blood enzymes. All the calculations were made using the SPSS © and t-test statistical method. In hematological findings nine parameters were revealed significant differences (P<0.05) with control group in t-test. It consisted of total WBC, Lymph, Neut, Hb and HCT, MCHC, AST, DL and total protein plasma. Also in total white blood cell count, Lymph and Neut had significant differences as compared with the control fish (P<0.05). Also blood serum components analysis revealed that only LDH and AST amount showed obvious significant differences (P<0.05). Regarding to results it could be concluded that hematological and biochemical studies could be a valuable tool for prognosis and primary diagnosis in some infectious diseases. So it could be recommended for monitoring and surveillance programs in coldwater hatchery health status in Iran.

생맥산의 식이가 Streptozocin으로 유도된 당뇨 Rat의 혈당과 혈청 성분 함량에 미치는 영향

이가 식이효율(FER), glucose, creatinine, cholesterol, triglycetide, HDL-cholesterol, 동맥경화지수(AI) 등에 미치는 영향을 조사하였다. 식이효율은 정상군이 5.94%로 가장 높았고, 당뇨대조군은 0.58%로 정상군에 비해 현격한 감소를 보였다. DA군과 DB군은 각각 3.65%, 3.38%로 다른 투여군보다 상대적으로 높은 수...

Spectroscopic study of the interaction of U(VI) with transferrin and albumin for speciation of U(VI) under blood serum conditions

The quantitative description of the interactions of uranium with blood serum components is of high relevance for a rational design of molecules suitable for in vivo chelation of uranium. We have determined the stability constants for the complexation of U(VI) with human serum transferrin and albumin by time-resolved laser-induced fluorescence spectroscopy and difference ultraviolet spectroscopy. Both proteins interact strongly with U(VI), forming ternary complexes with carbonate acting as a synergistic anion. Together with literature data describing the interaction of U(VI) with low molecular weight inorganic and organic serum components, the speciation of U(VI) in blood serum was calculated. In agreement with published experimental data, the model calculation shows that complexation with proteins and carbonate ion governs U(VI) speciation; 35% of U(VI) is bound to proteins and 65% to carbonate. Among the protein pool, albumin is the main protein interacting with U(VI). In addition, the results show that Ca(II) must be considered in the model as a competitive metal ion with respect to U(VI) for binding to albumin surface sites. Based on these findings several promising molecules for in vivo chelation of (230)U could be identified.

On the Transport of Vanadium in Blood Serum

The complexation of the VO(2+) ion in several systems that can model the physiological conditions of its transport in blood serum was studied using electron paramagnetic resonance (EPR) spectroscopy. Particularly, the ternary systems formed by (i) VO(2+) and two high-molecular-mass components of blood serum, human serum apo-transferrin (hTf) and human serum albumin (HSA); (ii) VO(2+), hTf, and bL; and (iii) VO(2+), HSA, and bL, where bL is one of the six most important low-molecular-mass bioligands of the blood serum (bL = lactate, citrate, oxalate, phosphate, glycine, or histidine), were examined. The results indicate that, in aqueous solution, transferrin is a stronger binder than albumin, and at the physiological ratio, most of the VO(2+) ion is present as (VO)(2)hTf, and a small amount as (VO)(2)(d)HSA, the dinuclear species formed by albumin where the two metal ions are interacting and the spin state S is 1. Among the bL ligands, only lactate and citrate are able to bind VO(2+) in the presence of transferrin or albumin, the others not interacting at all. Finally, the quaternary systems formed by (i) VO(2+), hTf, HSA, and lactate and (ii) VO(2+), hTf, HSA, and citrate were studied. In these cases, the results suggest that the predominant species is (VO)(2)hTf, followed by the mixed complexes VO(2+)-hTf-lactate or VO(2+)-hTf-citrate, whereas (VO)(2)(d)HSA and [(VO)(2)(citrH(-1))(2)](4-) are minor components at physiological pH. The conclusions of this study give new insights on how the VO(2+) ion distributes among the blood serum components and is transported in the plasma toward the target sites in the organism.

Integrated multi-sensor chip with photocured polymer membranes containing copolymerised plasticizer for direct pH, potassium, sodium and chloride ions determination in blood serum

An analytical system based on a sensor array with ion-selective field effect transistors (ISFETs) monolithically integrated in one chip covered with photocured polymer membranes containing copolymerised plasticizer and a sequential injection analysis (SIA) is shown to offer an automation of the analysis of blood serum components. For sequential injection system a custom made dual channel flow cell for the sensor array was developed. Optimisation of ion-sensitive membrane characteristics and calibration solution compositions were carried out. The system was used to analyze sodium, potassium, chloride ion contents in blood serum samples. The precision of the ion determination in samples was typical for potentiometic method with standard deviation of about 3–5%.

Mesenchymal stem cells expressing TRAIL lead to tumour growth inhibition in an experimental lung cancer model

Lung cancer is a major public health problem in the western world, and gene therapy strategies to tackle this disease systemically are often impaired by inefficient delivery of the vector to the tumour tissue. Some of the main factors inhibiting systemic delivery are found in the blood stream in the form of red and white blood cells (WBCs) and serum components. Mesenchymal stem cells (MSCs) have been shown to home to tumour sites and could potentially act as a shield and vehicle for a tumouricidal gene therapy vector. Here, we describe the ability of an adenoviral vector expressing TRAIL (Ad.TR) to transduce MSCs and show the apoptosis-inducing activity of these TRAIL-carrying MSCs on A549 lung carcinoma cells. Intriguingly, using MSCs transduced with Ad.enhanced-green-fluorescent-protein (EGFP) we could show transfer of viral DNA to cocultured A549 cells resulting in transgenic protein production in these cells, which was not inhibited by exposure of MSCs to human serum containing high levels of adenovirus neutralizing antibodies. Furthermore, Ad.TR-transduced MSCs were shown not to induce T-cell proliferation, which may have resulted in cytotoxic T-cell-mediated apoptosis induction in the Ad.TR-transduced MSCs. Apoptosis was also induced in A549 cells by Ad.TR-transduced MSCs in the presence of physiological concentrations of WBC, erythrocytes and sera from human donors that inhibit or neutralize adenovirus alone. Moreover, we could show tumour growth reduction with TRAIL-loaded MSCs in an A549 xenograft mouse model. This is the first study that demonstrates the potential therapeutic utility of Ad.TR-transduced MSCs in cancer cells and the stability of this vector in the context of the blood environment.

Serodiagnosis of Lyme borreliosis infection using surface plasmon resonance

Background Label-free biosensors are ideally suited for the direct monitoring of binding events without the need for additional labeling substances; however, their application in the field of serodiagnosis is not trivial. The major problem is the unspecific adsorption of blood serum components to the sensor surface. Methods A surface plasmon resonance (SPR) sensor has been used for the direct detection of Lyme borreliosis specific antibodies in blood serum. The combination of an optimal dilution factor with the addition of suitable detergents minimizes the unspecific adsorption. Serum samples from healthy donors and infected patients have been analyzed and the results were compared with a certified immunoassay and a western blot. Results A serum dilution of 1:20 in HBS-buffer with 0.05% Tween20 and 1 mg/mL carboxymethyl dextran reduces unspecific adsorption significantly and enables the identification of antibodies against the OspC/pepC10 antigen pair with a sensitivity of 92% and that against the VlsE/C6 pair with 81% sensitivity; the specificities are 82% and 86% respectively. Positive hits in the western blot could also be determined in the SPR-assay with a correlation of 96.5%. Conclusion The presented optical label-free technique has the potential for a precise and fast identification of pathogen-specific antibodies without the need for a secondary labeling antibody.

Blood serum components and serum protein test of Hybro-PG broilers of different ages

Blood serum samples of HYBRO PG broilers were analyzed, with 30 samples collected from 21-day-old broilers (G1), 30 from 35-day-old birds (G2), and 30 from 42-day-old birds (G3), with the aim of establishing normal values of some blood serum parameters. The activities of the enzymes gamma-glutamyl-transferase (GGT), aspartate aminotransferase (AST), creatine kinase (CK), alkaline phosphatase (ALP), and lactate dehydrogenase (LDH), serum levels of total calcium, calcium ion, phosphorus, sodium, potassium, magnesium, chlorides, creatinine, uric acid, triglycerides, cholesterol, total protein, albumin, total and indirect and direct bilirubin, and electrophoretic profile of serum proteins in acrylamide (SDS-PAGE) and agarose gel were determined. There was no influence of age on total bilirubin and albumin levels. All the other evaluated parameters presented differences in at least one age group. Protein electrophoretic profile also changed as a function of age. The obtained results can be considered as normal for the studied ages, and therefore be used as references for the interpretation of laboratory exams of broilers of this genetic line in the evaluated ages.

Regional differences in foraging of young-of-the-year Steller sea lions Eumetopias jubatus in Alaska: stable carbon and nitrogen isotope ratios in blood

Stable nitrogen and carbon isotope ratios were measured from red blood cell (RBC) and serum components from 9 mo old Steller sea lions Eumetopias jubatus captured during February and March 2000 and 2001 from the Gulf of Alaska (GOA; Region 1, n = 11), the eastern Aleutian Islands (Region 3, n = 5), and the central Aleutian Islands (Region 4, n = 5) to assess their foraging ecology. Isotope ratios from sea lions were compared with those from probable prey species and results were compared with those from a study demonstrating regional differences in the diets of juvenile and adult sea lions through the use of scat analysis. Discriminant analyses using the δ 15 N and δ 13 C values of each blood component as the discriminant functions accurately classified sea lions to the appropri- ate foraging regions as predicted by a previous study employing scat analysis with an accuracy of 90% for serum and 95% for RBCs. The δ 15 N values reflect a decrease in sea lion trophic position mov- ing east to west that is probably driven by changes in sea lion diet. The δ 13 C values demonstrated clear distinctions between foraging locations that are likely driven by known geographic carbon isotope patterns observed in the GOA and along the Aleutian archipelago. Our data present further evidence that, in the marine environment, δ 13 C values do not covary with δ 15 N values as a result of trophic enrichment, and are better determinants of foraging location than trophic position.

Magnetic resonance imaging of atherosclerosis by targeting extracellular matrix deposition with Gadofluorine M

As previously reported, Gadofluorine M-enhanced magnetic resonance imaging clearly demarcates atherosclerotic plaques from the normal vessel wall. To date, the underlying mechanism has remained unknown. Gadofluorine M is a gadolinium-containing macrocyclic contrast agent containing hydrophilic and hydrophobic moieties. To elucidate the mechanism of accumulation, fluorescently labeled and radioactively labeled derivates of Gadofluorine M were used to determine affinity and specificity of Gadofluorine M binding to blood serum and plaque components in vitro and for the distribution within the plaque of WHHL rabbits in vivo. Gadofluorine M binds to serum albumin, leading to a breakdown of micelles after intravenous injection. The affinity of Gadofluorine M to serum albumin is k(D) = 2 micromol/l. Gadofluorine then penetrates the atherosclerotic plaque while bound to albumin and then accumulates within the extracellular, fibrous parts of the plaque by binding to collagens, proteoglycans and tenascin, having the same affinity to these plaque constituents as to albumin. In contrast, weak binding was determined to LDL (k(D) = 2 mmol/l) and even no binding to hyaluronic acid. The driving force of binding and accumulation is the hydrophobic moiety of the molecules interacting with hydrophobic plaque materials. Thus, Gadofluorine M accumulates within the fibrous plaque or in the fibrous cap of a plaque containing high amounts of extracellular matrix components, but not in the lipid-rich areas. In combination with high-resolution MRI, Gadofluorine M might enable the detection of thin-cap fibroatheromas, also named the vulnerable plaque.

Spectral-luminescent manifestation of the damaging action of brain ischemia on blood serum components

With the aid of spectral-luminescent analysis, our hypothesis on the determining role of free-radical oxidation in damage of blood serum components (low-density lipoproteins) in ischemia has been confirmed. An increase in the luminescence intensity of the blood serum of animals that suffered from brain ischemia as against that of healthy animals is registered. Lipoperoxide free-radical damage of phospholipids of the amphipathic layer of low-density lipoproteins after an ischemic procedure has also been confirmed by fluorescent probes (rhodamine 6G and Nile Blue).

Conditions that influence bacterial luminescence in the presence of blood serum

Conditions that influence the luminescence of natural and recombinant luminescent bacteria in the presence of blood serum were studied. In general, blood serum quenched the luminescence of the marine Photobacterium phosphoreum and the recombinant Escherichia coli strains harboring the luminescent system genes of Photobacterium leiognathi, but enhanced the luminescence of the soil bacterium Photorhabdus luminescens Zm1 and the recombinant E. coli strain harboring the lux operon of P. luminescens Zm1. The quenching effect of blood serum increased with its concentration and the time and temperature of incubation. The components of blood serum that determine the degree and specificity of its action on bacterial luminescence were identified.

Selective removal of interference signals for near-infrared spectra of biomedical samples by using region orthogonal signal correction

New approach for chemometrics algorithm named region orthogonal signal correction (ROSC) has been introduced to improve the predictive ability of PLS models for biomedical components in blood serum developed from their NIR spectra in the 1280–1849 nm region. Firstly, a moving window partial least squares regression (MWPLSR) method was employed to locate the region due to water as a region of interference signals and to find the informative regions of glucose, albumin, cholesterol and triglyceride from NIR spectra of bovine serum samples. Next, a novel chemometrics method named searching combination moving window partial least squares (SCMWPLS) was used to optimize those informative regions. Then, the specific regions that contained the information of water, glucose, albumin, cholesterol and triglyceride were obtained. When an interested component in the bovine serum solution, such as glucose, albumin, cholesterol or triglyceride is being an analyte, the other three interests and water are considered as the interference factors. Thus, new approach for ROSC has employed for each specific region of interference signal to calculate the orthogonal components to the concentrations of analyte that were removed specifically from the NIR spectra of bovine serum in the region of 1280–1849 nm and the highest interference signal for model of analyte will be revealed. The comparison of PLS results for glucose, albumin, cholesterol and triglyceride built by using the whole region of original spectra and those developed by using the optimized regions suggested by SCMWPLS of original spectra, spectra treated OSC for orthogonal components of 1–3 and spectra treated ROSC using selected removing the highest interference signals from the spectra for orthogonal components of 1–3 are reported. It has been found that new approach of ROSC to remove the highest interference signal located by SCMWPLS improves of the performance of PLS modeling, yielding the lower RMSECV and smaller number of PLS factors.

Structural characterization and biological activities of an exopolysaccharide kefiran produced by Lactobacillus kefiranofaciens WT-2B(T).

Lactobacillus kefiranofaciens, isolated from kefir grains, produces an extracellular polysaccharide when cultured, not only in PYG10 medium but also in a liquid medium containing a rice hydrolysate that had been previously degraded by treatment with a glucoamylase. The maximum yield of the polysaccharide, using the rice hydrolysate as the medium, was 2.5 g/L after a 7-day culture period at pH 5.0 and 33 degrees C. Compositional analysis, methylation analysis, specific rotation, and (1)H and (13)C NMR spectroscopy revealed that the structures of polysaccharides obtained from these two different culture media are essentially identical. The polysaccharide is composed of a hexasaccharide repeating unit and, thus, is known as kefiran. The weight-average molecular weight and the z-average radius of gyration of a sample, purified from the rice hydrolysate medium, were determined to be 7.6 x 10(5) g/mol and 39.9 nm, respectively, by gel permeation chromatography equipped with a multiangle laser-light-scattering photometer. Changes in blood pressure and serum components were examined in SHRSP/Hos rats, using doses of 100 and 300 mg of kefiran/kg of rat. A suppression in the increase in blood pressure was observed in these rats after 30 days. This activity is discussed in terms of the concentration of serum components of the rat, with emphasis on lipid components such as cholesterols, triglycerides, and free fatty acids.

Reagentless Determination of Human Serum Components Using Infrared Absorption Spectroscopy

Simultaneous determination of concentrations for four major components in human blood serum was investigated using a Fourier-transform mid-infrared spectroscopy. Infrared spectra of human blood serum were measured in 8.404 ∼ 10.25 <TEX>${\mu}m$</TEX> range where the highest absorption peaks of glucose are located. A partial least square (PLS) algorithm was utilized to establish a calibration model for determining total protein, albumin, globulin and glucose levels which are commonly measured metabolites. The standard error of cross validation obtained from our multivariate calibration model was 0.24 g/dL for total protein, 0.15 g/dL for albumin, 0.17 g/dL for globulin, and 6.68 mg/dL for glucose, which are comparable with or meet the criteria for clinical use. The results indicate that the infrared absorption spectroscopy can be used to predict the concentrations of clinically important metabolites without going through a chemical process with a reagent.

Interaction between the low molecular mass components of blood serum and the VO(iv)–DHP system (DHP = 1,2-dimethyl-3-hydroxy-4(1H)-pyridinone)

In order to estimate the impact of the low molecular mass (l.m.m.) VO(IV) binders of blood serum on the potentially insulin-enhancing drug [VO(DHP)2] [DHP = 1,2-dimethyl-3-hydroxy-4(1H)-pyridinone], the speciation in the binary system VO(IV)–DHP and in the ternary systems VO–DHP–ligand B (B = oxalate, lactate, citrate or phosphate) was studied by pH-potentiometry at 25.0 °C and at an ionic strength I = 0.2 mol dm−3 (KCl). The binding modes of the complexes formed were determined by spectroscopic (electronic absorption and EPR) techniques. DHP was found to form stable mono and bis complexes via the coordination of (O,O) chelate(s). Through displacement of the oxo group of VO(IV), the tris complex is also formed, especially at a high excess of ligand. The results in the ternary systems demonstrate that, at physiological pH, none of the B ligands can compete with DHP; [VO(DHP)2] therefore seems to remain almost completely intact, even in the presence of citrate, the strongest competitor among these B ligands. These findings indicate that, for DHP, unlike maltol or picolinic acid, ternary complex formation and thus transformation reactions with the l.m.m. binders of biofluids, is almost negligible. From among the three carrier molecules, only DHP can efficiently compete with serum transferrin for binding of VO(IV).