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On the Possibility of Indirect Determination of the Glass Transition Temperature of Proteins from Viscosity Measurements and Avramov's Model

-lactoglobulin solutions from viscometry approach. Polish J. Environ. Stud. 15 , 88-90. Monkos K. (2009). Activation energy of viscous flow for some globular and non-globular proteins obtained from viscosity measurements and modified Arrhenius equation. Ann. Acad. Med. Siles. 63 , 27-38. Monkos K. (2011). A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity f or glass-forming liquids. Curr. Top. Biophys. 34 , 1-9. Monkos K. (2013). A viscometric approach of pH effect on hydrodynamic

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Nanoparticle Tracking Analysis of Latex Standardized Beads

References Bangs Laboratories, Inc. (9.02.2014) http://www.bangslabs.com. Berne B.J., Pecora R., (1976) Dynamic Light Scattering: with Applications to Chemistry, Biology, and physics, Wiley, New York. Boyd RD, Pichaimuthu SK., Cuenat A. (2011) New approach to inter-technique comparisons for nanoparticle size measurements; using atomic force microscopy, nanoparticle tracking analysis and dynamic light scattering. Colloids and Surfaces A: Physicochemical and Engineering Aspects , 387 , 35-42. Chatterjee J., Haik Y., Chen C. J. (2001) Modification

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EPR Study of Paramagnetic Centers in Human Blood

Copper Measurements in Human Normal Control and Cancer Patient, Cancer Res. 43(7) , 3447-3450. Kouoh Elombo F., Radosevich M., Poulle M., Descamps J., Chtourou S., Burnouf T., Catteau J. P., Bernier J. L. & Cotelle N. (2000). Purification of human ceruloplasmin as a by- product of C1-inhibitor. Biol. Pharm. Bull. 23 , 1406-1409. Krzyminiewski R., Kruczyński Z., Dobosz B., Zając A., Mackiewicz A., Leporowska E. & Folwaczna S. (2011). EPR Study of Iron Ion Complexes in Human Blood. Appl. Magn. Reson. 40 , 321-330. Kubiak

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Pulse Wave Shape Analysis of the Cardiovascular System Using High Signal Resolution

. (2010), Estimation of Three- and Four-Element Windkessel Parameters Using Subspace Model Identification. Biomedical Engineering; 57. 7: 1531 - 38. Matthys K. S., Alastruey J., Peiro J., Khir A. W., Segers P., Verdonck P. R., Parker K. H., Sherwin S. J. (2007) Pulse wave propagation in a model human arterial network: Assessment of 1-D numerical simulations against in vitro measurements. Journal of Biomechanics; 40: 3476-86. Krzyminiewski R., Szymił A., Dobosz B., Majewski M. (2011c), HSR-PW as a method of patient monitoring during and after short intravenous

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A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids

-310. Monkos K. (2008). Analysis of the viscosity-temperature-concentration dependence for dimeric bovine β-lactoglobulin aqueous solutions on the basis of the Vogel-Tammann-Fulcher's equation. Curr. Top. Biophys.   31 , 16-24. Monkos K., Turczynski B. (1991). Determination of the axial ratio of globular proteins in aqueous solution using viscometric measurements. Int. J. Biol. Macromol.   13 , 341-344. Pamies R., Hernández J. G., del Carmel López Martínez M., Garcia de la Torre J. (2008). Determination of intrinsic

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Testing Sorption Properties of Halloysite by Means of the Laser Interferometry Method

through cellulose biomembrane in the presence of Proteus vulgaris O25 lipopolysaccharide. J. Membrane Sci. , 299 , 268-275. Arabski M., Wąsik S., Dworecki K., Kaca W. (2009b). Laser interferometric and cultivation methods for measurement of colistin/ampicilin and saponin interactions with smooth and rough of Proteus mirabilis lipopolysaccharides and cells. J. Microbiol. Methods , 77 , 178-83. Del Rey-Bueno F., Romero-Carballo J., Villafranca-Sanchez E., Garcia-Rodriguez A., Sebastian-Pardo E.N. (1989). Adsorption of ammonia over activated at different

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The Glass Transition Temperature and Temperature Dependence of Activation Energy of Viscous Flow of Ovalbumin

solution conformations using viscometric measurements. [In:] Uversky V. & Permyakov E. (eds.), Methods in protein structure and stability analysis, Nova Science Publishers, New York, pp. 355-387. Monkos K. (2011a). A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids. Curr. Top. Biophys. 34, 1-9. Monkos K. (2011b). Temperature behavior of viscosity flow with proteins. Gen. Physiol. Biophys. 30, 121-129. Monkos K

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Interaction of plant alkaloid, berberine, with zwitterionic and negatively charged phospholipid bilayers

-527. Hu Y. J., Ou-Yang Y., Dai C. M., Liu Y. & Xiao X. H. (2010). Binding of berberine to bovine serum albumin: spectroscopic approach. Mol. Biol. Rep. , 37 , 3827-3832. Huang C. Z., Feng P., Li Y. F., Tan K. J. & Wang H. Y. (2005). Adsorption of penicillin-berberine ion associates at a water/tetrachloromethane interface and determination of penicillin based on total internal-reflected resonance light scattering measurements. Anal. Chim. Acta , 538 , 337-343. Imanshahidi M. & Hosseinzadeh H. (2008). Pharmacological

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Dynamic Light Scattering Investigation of Pnipam-Co-Maa Microgel Solution

The paper presents results of a study of the effect of the environment temperature and pH on the size of particles based on poly N (isopropylacrylamide) chain. The tested substance was the copolymer PNIPAM-co-MAA. The particle size measurements were performed by dynamic light scattering. It was found that the copolymer tested reacts specifically to temperature increase by shrinking more than two times. Important for stabilization of the structure are the chemical groups -COOH present in methacrylic acid that undergoes dissociation. Gradual increase in temperature results in a decrease in the dissociation constant, in binding of protons and thus causes shrinkage of the entire particle. It was also shown that PNIPAM-co-MAA in high concentrations undergoes crystallization.

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Peptides conformational changes of the erythrocyte membrane induced by organometallic tin compounds

Peptides conformational changes of the erythrocyte membrane induced by organometallic tin compounds

The paper presents the results of a study on the effect of selected organic chlorides of tin on peptide conformations of erythrocyte ghosts from pig blood. The following compounds were used: dibutyltin dichloride (DBT), tributyltin chloride (TBT), diphenyltin dichloride (DPhT) and triphenyltin chloride (TPhT). Peptide conformation changes were determined on the basis of measurements done with the ATR FTIR technique. This method made it possible to measure the percent share of a peptide with specified conformation in the whole amount of the peptides in the membranes studied. The investigation showed that all the tin organic compounds studied cause a several-percent decrease in the quantities of both the peptides with the α-helix and turn conformation, and about a 20% increase in ghost peptides with β-sheet conformation. It seems that the changes observed can cause disturbances in the function of proteins and, consequently, the activity of the membrane; and this may be one of the aspects of the toxic properties of organotins.

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