Response of hydrogen bonding to low-intensity 50 Hz electromagnetic field in typical proteins in bi-distilled water solution

Samples of hemoglobin and bovine serum albumin in different bi-distilled water solutions were exposed to a 50?Hz electromagnetic field at the intensity of 1?mT to investigate the response of hydrogen bonding to the applied field after exposure of 3?h by means of Fourier Transform Infrared spectroscopy. Spectral analysis evidenced a significant decrease in the absorbance signal of the Amide I vibration in exposed samples of hemoglobin and bovine serum albumin water solutions. In addition, Fourier self-deconvolution analysis and min-max normalization applied in the mid-infrared region to exposed and unexposed hemoglobin samples revealed a significant increase in the absorbance signal of the Amide II band and an up-shift toward the high energies of 1.5?cm^?1 after exposure. Similar findings were observed after exposure of bovine serum albumin. These results can be easily explained assuming that hydrogen bonding in the secondary structure of these proteins in bi-distilled water solutions was enhanced after exposure to 50?Hz electromagnetic field.     

Preparation and recognition of surface molecularly imprinted core-shell microbeads for protein in aqueous solutions

In this paper, a surface molecular imprinting technique was reported for preparing core-shell microbeads of protein imprinting, and bovine hemoglobin or bovine serum albumin were used as model proteins for studying the imprinted core-shell microbeads. 3-Aminophenylboronic acid (APBA) was polymerized onto the surface of polystyrene microbead in the presence of the protein templates to create protein-imprinted core-shell microbeads. The various samples were characterized using scanning electron microscopy (SEM), transmission electron microscopy (TEM), Raman spectroscopy, X-ray photoelectron spectroscopy (XPS) and Brunauer-Emmett-Teller (BET) methods. The effect of pH on rebinding of the template hemoglobin, the specific binding and selective recognition were studied for the imprinted microbeads. The results show that the bovine hemoglobin-imprinted core-shell microbeads were successfully created. The shell was a sort of imprinted thin films with porous structure and larger surface areas. The imprinted microbeads have good selectivity for templates and high stability. Due to the recognition sites locating at or closing to the surface, these imprinted microbeads have good property of mass-transport. Unfortunately, the imprint technology was not successfully applied to imprinting bovine serum albumin (BSA).     

Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

We have studied the fluorescent properties of flavonols (quercetin, fisetin, morin, rutin) with the aim of studying possible interaction with hemoglobin and bovine serum albumin (BSA). We observed an increase in the intensity of intrinsic fluorescence for all the flavonols except rutin in the presence of BSA. From the changes in the fluorescence spectra, we concluded that tautomeric forms are formed on interaction with hemoglobin. We determined the interconnection between the structure of related flavonols and their fluorescent properties on interaction with proteins, and we determined the binding constants for binding with BSA and hemoglobin. __________ Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 74, No. 5, pp. 659–664, September–October, 2007.     

A broad-band single pulse technique for ultrasound absorption studies of aqueous solutions in the frequency range 200 kHz–1 MHz

A single pulse time-domain technique is described for determining, via Fourier transform methods, the compressional wave ultrasound absorption coefficient in liquids contained in spherical reverberators over a frequency range from ≈ 200 kHz to 1 MHz. Only modest data storage and computational facilities are required. Such a technique offers an advantage over variable continuous frequency methods in that data for a given frequency range can be acquired ‘instantaneously’ and thus it is possible to monitor ultrasound absorption in time-varying systems. The method is illustrated by provision of absorption data in the frequency range 200 kHz–1 MHz for out-gassed water, aqueous solutions of the electrolyte cobaltous sulphate, with and without gas bubbles, and for the protein bovine serum albumin under conditions of acid pH obtained using spherical reverberators of 100 and 250 ml capacity.     

Determination of the parameters of the rotational diffusion of complexes of serum albumins with Triton X-100 from analysis of tryptophan fluorescence

The rotational diffusion of complexes of human serum albumin (HSA) and bovine serum albumin (BSA) with neutral surfactant Triton X-100 is study by analyzing the polarized tryptophan fluorescence and its parameters are determined (rotational relaxation time, diffusion coefficient, effective radius). Similarities in the solubilization of both proteins are revealed: an effective solubilization BSA and HSA in solutions containing neutral surfactant Triton X-100 is achieved at concentration of the latter of 0.3 mM, slightly greater than its critical micelle concentration (0.25 mM), with the most significant effect taking place at pH 5.0, a value close to the isoelectric points of the proteins.     

Ultrasonic absorption of bovine serum albumin solutions in the frequency range 60 to 160 kHz

The ultrasonic absorption of the globular protein bovine serum albumin in aqueous solution has been measured in the frequency range 60 to 160 kHz using a 2-1 spherical resonator. The effect of pH change and of the denaturants urea, guanidine hydrochloride, and sodium dodecyl sulfate on the absorption loss has been studied. It is concluded that a significant ultrasonic absorption process exists which is related to structural helix-coil transition equilibria. For native protein the maximum loss appears to occur at a frequency at least as low as 70 kHz for a pH of about 4.2. This loss process is distinct from those arising from proton-transfer equilibria perturbations which are manifest at pH 3.2 and 11.6 and at peak frequencies of 400 kHz and above.     

光谱法研究酸度对一种白杨素衍生物与牛血清白蛋白相互作用的影响

在3种酸度条件下,采用多种光谱技术对一种白杨素衍生物和牛血清白蛋白的相互作用进行了研究.结果表明该衍生物和牛血清白蛋白可形成基态复合物,静态、动态猝灭方式同时存在,以静态猝灭为主.通过计算获得了在不同温度及酸度条件下的结合常数及结合位点数.该衍生物在碱性条件下和牛血清白蛋白的结合能力较强.在pH 7.40的生理条件下,...     

Ultrasonic spectroscopy in bovine serum albumin solutions

Ultrasonic absorption and velocity spectra in bovine serum albumin (BSA) aqueous solutions have been measured at 20 degrees C over the broad frequency range 0.1-1600 MHz in the pH range 1.5-13.2. Five different techniques were used: the plano-concave resonator, plano-plano resonator, pulse-echo overlap, Bragg reflection, and high-resolution Bragg reflection methods. The absorption spectrum at neutral pH was well fitted to the relaxation curve assuming a distribution of relaxation frequency with a high-frequency cutoff and long low-frequency tail. The relaxation behavior was interpreted in terms of various degrees of hydration of BSA molecules. At acid pH's, excess absorption over that at pH 7 was explained by double relaxation. The pH dependences of the relaxation frequency and maximum absorption per wavelength showed that the relaxation at about 200 kHz was related to the expansion of molecules and that at 2 MHz resulted from the proton transfer reaction of carboxyl group. At alkaline pH's, the excess absorption was explained by triple relaxation. The relaxation at about 200 kHz was associated with a helix-coil transition, and the two relaxations at 2 and 15 MHz were attributed to the proton transfer reactions of phenolic and amino groups, respectively. The rate constants and volume changes associated with these processes were estimated.     

Mutual information theory for biomedical applications: Estimation of three protein-adsorbed dialysis membranes

Protein-adsorbed dialysis membranes are evaluated with time-of-flight secondary ion mass spectrometry (TOF-SIMS) chemical imaging technique. Protein adsorption causing permeability change is one of big issues in the development of dialysis membranes. Bovine serum albumin adsorption onto three kinds of dialysis membranes has been evaluated with TOF-SIMS. In the present study three kinds of proteins, bovine serum albumin, α-chymotripsinogen A, and cytochrome C adsorbed onto hollow-fiber dialysis membranes, were measured by means of TOF-SIMS and then TOF-SIMS spectra were analyzed using mutual information. Then specific peaks of fragment ions related to α-chymotripsinogen A and bovine serum albumin were found, respectively. In this condition, however, specific peaks to cytochrome C were not able to find compared with other samples. Finally, chemical images of α-chymotripsinogen A and bovine serum albumin, respectively, adsorbed onto the membranes with co-existing proteins were obtained. The results of TOF-SIMS images of the proteins on the membranes show different tendency of adsorption depending on co-existing proteins. Further study is needed to study more detailed protein adsorption onto the membranes with co-existing proteins.     

The influence of molecular structure of protein on the acoustic nonlinearity parameter B/A

I.IntroductionAcousticnonlinearityparameterB/Adescrjbesthenonlilleareffectsofasoundwavetrav-ellingthroughamedium.Withtheapplicationofhighmowerultrasonicwavetomedicine,thenonlineareffectsbecomemoreandmoreimportant.EspeciallybecauseB/Aissensitivetothepathologicalstateofbiologicaltissues[1-2])thisprovidesprospectiveapplicationinmedicaldiagnosis.Atpresent,thestudyinthisareaemphasizesontwoaspects.OneistodevelopnewmedicalimagingtechniquesbyusingthisnonlinearityparameterB/Al1'3-'];theotheristostu…     

Preparation and water relaxation properties of proteins labeled with paramagnetic metal chelates

The proteins bovine serum albumin (BSA) and bovine immunoglobulin (IgG) have been labeled with paramagnetic gadolinium (III) and manganese (II) complexes using the bifunctional chelate approach. Diethylenetriaminepentaacetic acid (DTPA) and ethylenediaminetetraacetic acid (EDTA) were attached to several free amino groups on the proteins using cyclic anhydride forms of these ligands. The incorporation of the metal ions Gd+3 and Mn+2 into the chelating groups yielded highly paramagnetic proteins. The water relaxation ability (or relaxivity) of the protein-bound chelates at 20 MHz was found to be superior to that of the free metal complexes. Differences in relaxivity between the DTPA and EDTA conjugates could largely be accounted for by differences in the metal ion exposure to water. This labeling technique can be used in the preparation of intravascular NMR contrast agents (like paramagnetically-labeled human serum albumin) or target-specific agents (labeled monoclonal antibodies or fibrinogen).     

Conformation transitions of blood proteins under influence of physical factors on microwave dielectric method

In this article, the influence of γ-irradiation and temperature on albumin and fibrinogen conformation and dielectric properties of protein solutions have been studied by the microwave dielectric method. Both the values of the real part ε′ (dielectric permittivity) and the imaginary part ε″ (dielectric losses) of the complex dielectric permittivity of the aqueous solution of bovine serum albumin and human fibrinogen as functions of temperature and γ-irradiation dose have been obtained. The time of dielectric relaxation of water molecules in the protein solutions was calculated. The hydration of the albumin and fibrinogen molecules was determined. The temperature dependencies of hydration are non-monotonous and have a number of characteristic features at the temperatures 30-34 and 44-47 °C for serum albumin, and 24 and 32 °C for fibrinogen.     

Laser fluorimetry of proteins containing one and two tryptophan residues

The true molecular photophysical parameters’ values of tryptophan residues in single-tryptophan-containing and two-tryptophan-containing proteins (by the example of human serum albumin and bovine serum albumin) have been determined for the first time with the use of the authors’ suggested algorithm. The algorthm is based on the simultaneous use of nonlinear and kinetic-laser fluorimetry. The obtained result opens up new approaches in the monitoring of living systems and other objects, containing single fluorophores and localized pairs of fluorophores.     

pH协同血清白蛋白对单个活态人红细胞作用的拉曼光谱研究

红细胞是维持生命最重要的细胞之一,pH是影响其结构功能的重要因素。 结合人血液中存在血清白蛋白,且可能会对红细胞起作用的特点,在模拟人体内血液中血清白蛋白与血红蛋白摩尔比值的条件下,研究pH协同血清白蛋白对单个活态人红细胞的形态,细胞膜变形能力及胞内血红蛋白结构变化的影响。 结果显示,不同pH下,红细胞的表面形态、 膜变形能力的变化规律与其胞内血红蛋白结构的变化有关：在pH 4.14,4.76,10.18时,红细胞胞内血红蛋白螺旋结构的减少、 疏水性氨基酸的暴露,血红素珠蛋白结合状态的改变,影响了血红蛋白结构的稳定性,从而导致红细胞的结构发生变化,其形态、 膜变形能力与正常值相比,变化结果显著。 而在pH 6.51和7.80下,血红蛋白的拉曼谱结果并未发现有上述变化情况,胞内血红蛋白的结构没有发生改变,红细胞的形态、 膜变形能力也接近于正常值。 在pH 5.49和8.76下,红细胞的表面形态和膜变形能力都有不同程度的变差,但其胞内血红蛋白的结构并没有改变,提示红细胞的形态和变形能力的改变可能是可逆的。 结果表明,pH协同血清白蛋白的作用下,血清白蛋白能对红细胞起保护作用,增强红细胞调节、 缓冲环境pH变化的能力。 研究结果全面地揭示了在模拟人体内血液中血清白蛋白与血红蛋白摩尔比值的情况下,红细胞结构功能的变化情况,不仅有助于阐明红细胞在有关生理、 病理状态下的结构与功能的变化,而且对其临床表现与有关防治对策都有重要的指导意义。     

Fluorescence resonance energy transfer: A promising tool for investigation of the interaction between 1-anthracene sulphonate and serum albumins

This present investigation has revealed that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors for exploring the interaction of fluorescent probe 1-anthracene sulphonate (1-AS) with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA).We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to 1-AS, for the study of relaxation dynamics of biological molecules.     

Intramolecular motions in proteins and model polymers on Moessbauer Spectroscopy and Rayleigh Scattering of Moessbauer Radiation data

In the survey, the scales and correlation times of motion on different levels are considered: iron atoms in active centre of myoglobin and hemoglobin, iron containing core in iron storage proteins and model polymer systems, and the average fragmental motion of a protein globule of myoglobin and human serum albumin. The models of intramolecular protein mobility have been drawn.     

Fluorescence Study of Sinapic Acid Interaction with Bovine Serum Albumin and Egg Albumin

The mechanism of interaction of protein with compounds used for preparation of matrices for matrix-assisted laser desorption ionization–mass spectrometry (MALDI-MS) methods is unknown. This paper reports the investigation of this mechanism for sinapic acid and bovine serum albumin and egg albumin. To examine these interactions in water a fluorescence method was applied. Sinapic acid can exist in three different forms, depending on pH: undissociated and with one or two deprotonated groups. pK_as of these states are: 4.47 for the COOH group and 9.21 for the OH group [1]. Therefore the interactions were examined at pH: 2.0, 6.4, and 10.5. The results show that sinapic acid at pH 10.5, being a bivalent anion, does not form any complex with these two proteins. At pH 2.0, sinapic acid, being undissociated, interacts weakly with egg albumin. Sinapic acid does not interact with bovine serum albumin at this pH. At pH 6.4, sinapic acid interacts only with bovine serum albumin. Parameters of the sinapic acid and bovine serum albumin complex were calculated based on the theory of multiple equlibria: the total number of binding sites, N = 15; the binding constant, K = 600 M ^–1; and the Hill's coefficient, j = 0.97. These parameters indicate (but not definitively because a large saturation was not obtained) that this is a simple binding of sinapic acid to bovine serum albumin with the binding sites of the same type.     

Protein imprinted polymer using acryloyl-β-cyclodextrin and acrylamide as monomers

A novel protein imprinted polymer was prepared using acryloyl-β-cyclodextrin (β-CD) and acrylamide as monomers on the surface of silica gel. The bovine hemoglobin was used as template and β-CD was allowed to self-assemble with the template protein through hydrogen bonding and hydrophobic interaction. Polymerization was carried out in the presence of acrylamide as an assistant monomer, which resulted in a novel protein imprinted polymer. After removing the template, imprinted cavities with the shape and spatial distribution of functional groups were formed. Bovine serum albumin (BSA) cytochrome c (Cyt) and lysozyme (Lyz) were employed as non-template proteins to test the imprinting effect and the specific binding of bovine hemoglobin to the polymer. The results of the adsorption experiments indicated that such protein imprinted polymer, which was synthesized with β-CD and acrylamide as monomers, could selectively recognize the template protein.     

SiO2纳米粒子在毛细管电泳分离蛋白质中的应用

将SiO2纳米粒子作为添加剂用于溶菌酶、牛血清白蛋白、牛血红蛋白的毛细管电泳(CE)分离研究.对影响3种蛋白质分离的因素如缓冲溶液的浓度,SiO2纳米粒子、聚合物PVP、乙腈的含量,及分离电压、温度等进行了考察,得到最佳分离条件,即50mmol/L NaH2PO4-10mmol/L H3PO4缓冲溶液(pH=2.8),...